8OXM: ATM(Q2971A) activated by oxidative stress

ATM(Q2971A) activated by oxidative stress in complex with Mg AMP-PNP and p53 peptide. Determined by electron microscopy at 3.3 Å resolution. Released 27 Sept 2023.

Method
Electron microscopy
Resolution
3.3 Å
Organism
Homo sapiens
Chains
4
Atoms
44,174
Mol. weight
733.93 kDa
Ligands
ANP, MG, ZN
Released
27 Sept 2023

Explore 8OXM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8OXM contains 335 α-helices and 44 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 165 helices, 21 β-strands

ElementResiduesLengthSheet
α-helix6-1611
α-helix20-3314
α-helix36-416
α-helix57-7317
α-helix89-10820
α-helix117-12812
α-helix135-14410
α-helix145-1495
α-helix153-1586
α-helix161-17515
α-helix184-20118
α-helix207-2093
α-helix210-22011
α-helix229-24315
α-helix248-26720
α-helix273-29018
α-helix298-3003
α-helix306-32318
α-helix340-3423
α-helix343-35614
α-helix393-40210
α-helix410-42213
α-helix424-4263
α-helix432-44211
α-helix451-46717
α-helix474-49118
α-helix501-51414
α-helix521-5266
α-helix536-54712
α-helix572-5809
α-helix597-6004
α-helix608-6169
β-strand61711
α-helix620-6289
α-helix646-65611
β-strand68211
α-helix684-70320
α-helix713-73119
α-helix737-7426
α-helix744-76522
α-helix773-78614
α-helix795-80612
α-helix809-82315
α-helix881-8833
α-helix887-8893
α-helix892-91120
α-helix920-93011
α-helix941-95313
α-helix960-9623
α-helix963-9708
α-helix973-9797
α-helix984-99411
α-helix995-9973
α-helix998-10025
α-helix1009-103022
α-helix1036-105217
β-strand1060-106342
β-strand1066-106942
α-helix1070-10767
α-helix1077-10793
α-helix1083-109210
α-helix1093-10964
α-helix1113-113220
α-helix1143-116422
α-helix1169-118214
α-helix1187-120115
α-helix1206-12116
α-helix1214-12229
α-helix1236-12383
α-helix1244-126017
α-helix1265-12728
α-helix1279-12857
α-helix1287-12948
α-helix1295-12984
α-helix1306-132217
α-helix1332-13387
α-helix1341-13499
β-strand135113
β-strand138113
α-helix1383-139614
α-helix1404-14085
α-helix1413-142816
α-helix1432-145019
α-helix1458-14603
α-helix1461-147717
α-helix1491-150818
α-helix1518-15236
α-helix1525-15273
α-helix1532-154312
α-helix1544-15485
α-helix1553-15608
α-helix1569-15713
α-helix1572-15765
α-helix1579-15824
α-helix1590-160314
α-helix1611-162313
α-helix1627-16348
α-helix1639-16413
α-helix1643-165816
α-helix1664-167613
β-strand168714
α-helix1694-17029
α-helix1706-172116
α-helix1727-174014
α-helix1744-175310
α-helix1760-17645
α-helix1792-17954
α-helix1802-181514
α-helix1828-18314
α-helix1835-185117
α-helix1857-187317
α-helix1903-191715
α-helix1920-19212
α-helix1927-19304
α-helix1938-194710
α-helix1951-197323
α-helix1986-199611
α-helix2001-201111
α-helix2018-20214
α-helix2029-203810
α-helix2042-205110
α-helix2057-207014
α-helix2075-208713
α-helix2093-210513
α-helix2124-213613
α-helix2141-216020
β-strand216514
α-helix2169-218820
α-helix2195-221117
α-helix2217-223620
α-helix2242-226322
α-helix2269-228113
α-helix2290-230112
α-helix2305-232117
α-helix2328-234821
α-helix2353-23564
α-helix2357-23615
α-helix2362-23709
α-helix2377-240630
α-helix2408-242922
α-helix2436-247540
α-helix2481-24833
α-helix2484-24918
α-helix2498-25069
α-helix2508-25103
α-helix2513-25153
α-helix2520-25245
α-helix2535-255117
α-helix2557-25648
α-helix2568-25725
α-helix2593-261220
α-helix2614-263219
α-helix2636-26383
β-strand2645-264625
α-helix2647-26482
α-helix2652-26554
β-strand266316
β-strand268216
β-strand2683-268647
β-strand2689-269025
β-strand2691-269227
β-strand2700-270677
β-strand2711-271887
α-helix2723-274119
α-helix2743-27486
β-strand2757-275937
β-strand2764-276857
α-helix2769-27702
β-strand2773-277538
α-helix2776-27805
α-helix2787-27915
α-helix2796-27972
α-helix2798-280811
α-helix2813-282513
α-helix2833-28364
α-helix2842-286625
α-helix2873-28753
β-strand2876-287948
β-strand2885-288738
α-helix2912-29187
α-helix2926-294015
α-helix2942-29498
α-helix3004-301815
α-helix3028-304013
α-helix3042-30465
α-helix3050-30523
Chain B: 170 helices, 23 β-strands
ElementResiduesLengthSheet
α-helix6-1611
α-helix20-3314
α-helix36-416
α-helix57-7317
α-helix89-10820
α-helix117-12812
α-helix135-14410
α-helix145-1495
α-helix153-1575
α-helix161-17515
α-helix184-20118
α-helix207-2093
α-helix210-22011
α-helix229-24315
α-helix248-26720
α-helix273-29018
α-helix292-2943
α-helix298-3003
α-helix306-32318
α-helix340-3423
α-helix343-35614
α-helix393-40210
α-helix410-42213
α-helix424-4263
α-helix432-44211
α-helix451-46717
α-helix474-49219
α-helix498-5003
α-helix501-51414
α-helix521-5266
α-helix536-54712
α-helix572-5809
α-helix597-6004
α-helix608-6158
β-strand61719
α-helix620-6278
α-helix646-65611
β-strand68219
α-helix684-70320
α-helix713-73119
α-helix737-7415
α-helix744-76522
α-helix773-78614
α-helix795-80612
α-helix809-82315
α-helix881-8833
α-helix887-8893
α-helix892-91019
α-helix911-9133
α-helix920-93011
α-helix941-95313
α-helix960-9623
α-helix963-9708
α-helix973-9797
α-helix984-99411
α-helix998-10014
α-helix1009-103022
α-helix1036-105217
β-strand1060-1063410
β-strand1066-1069410
α-helix1070-10767
α-helix1077-10793
α-helix1083-109210
α-helix1093-10953
α-helix1113-113220
α-helix1143-116422
α-helix1169-118214
α-helix1187-120115
α-helix1206-12116
α-helix1214-122411
β-strand1226111
β-strand1229111
α-helix1231-12333
α-helix1236-12383
α-helix1244-126118
α-helix1265-127410
α-helix1279-12857
α-helix1287-12948
α-helix1295-12984
α-helix1306-132217
α-helix1328-13314
α-helix1332-13387
α-helix1340-134910
β-strand1351112
β-strand1381112
α-helix1383-139614
α-helix1404-14085
α-helix1413-142816
α-helix1432-145019
α-helix1464-147714
α-helix1491-150818
α-helix1518-15236
α-helix1525-15284
α-helix1532-154312
α-helix1544-15485
α-helix1553-15608
α-helix1569-15713
α-helix1572-158211
α-helix1590-160314
α-helix1611-162313
α-helix1627-16348
α-helix1639-16413
α-helix1643-165816
α-helix1664-167613
β-strand1687113
α-helix1694-17029
α-helix1706-172116
α-helix1727-174014
α-helix1744-175310
α-helix1760-17645
α-helix1765-17673
α-helix1792-17954
α-helix1802-181514
α-helix1828-18314
α-helix1835-185117
α-helix1857-187317
α-helix1903-191715
α-helix1920-19212
α-helix1927-19304
α-helix1938-194710
α-helix1951-197323
α-helix1986-199611
α-helix2001-201111
α-helix2019-20213
α-helix2029-203810
α-helix2042-205110
α-helix2057-207014
α-helix2075-208713
α-helix2093-210513
α-helix2124-213613
α-helix2140-216021
β-strand2165113
α-helix2169-218820
α-helix2195-221117
α-helix2217-223620
α-helix2242-226322
α-helix2269-228113
α-helix2291-230111
α-helix2305-232117
α-helix2328-234821
α-helix2353-23564
α-helix2357-23615
α-helix2362-23709
α-helix2377-240529
α-helix2408-242922
α-helix2436-247540
α-helix2481-24833
α-helix2484-24896
α-helix2498-25069
α-helix2508-25103
α-helix2513-25153
α-helix2520-25245
α-helix2535-255117
α-helix2557-25648
α-helix2568-25725
α-helix2593-261018
α-helix2614-263219
α-helix2636-26383
β-strand2645-2646214
α-helix2647-26482
α-helix2652-26554
β-strand2663115
β-strand2682115
β-strand2683-2686416
β-strand2689-2690214
β-strand2691-2692216
β-strand2700-2706716
β-strand2711-2716616
α-helix2723-274119
α-helix2743-27486
β-strand2757-2759316
β-strand2765-2768416
α-helix2769-27702
β-strand2773-2775317
α-helix2776-27805
α-helix2787-27915
α-helix2796-27972
α-helix2798-280811
α-helix2813-282513
α-helix2831-28333
α-helix2834-28385
α-helix2842-286625
α-helix2873-28753
β-strand2876-2879417
β-strand2885-2887317
α-helix2912-29176
α-helix2922-29243
α-helix2926-294015
α-helix2942-29498
α-helix3004-301815
α-helix3028-304013
α-helix3042-30465
α-helix3050-30523

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Cellular tumor antigen p53E, Fprotein12Homo sapiensP04637 (AlphaFold model)
Serine-protein kinase ATMA, Bprotein3184Homo sapiensQ13315
Sequence of entity 1 (E, F), FASTA
>8OXM_1 Cellular tumor antigen p53 (chains E, F)
EPPLSQETFSDL
Sequence of entity 2 (A, B), FASTA
>8OXM_2 Serine-protein kinase ATM (chains A, B)
MDYKDDDDKHMGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFM
LGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLEGG
SAGSGSASMSLVLNDLLICCRQLEHDRATERKKEVEKFKRLIRDPETIKHLDRHSDSKQG
KYLNWDAVFRFLQKYIQKETECLRIAKPNVSASTQASRQKKMQEISSLVKYFIKCANRRA
PRLKCQELLNYIMDTVKDSSNGAIYGADCSNILLKDILSVRKYWCEISQQQWLELFSVYF
RLYLKPSQDVHRVLVARIIHAVTKGCCSQTDGLNSKFLDFFSKAIQCARQEKSSSGLNHI
LAALTIFLKTLAVNFRIRVCELGDEILPTLLYIWTQHRLNDSLKEVIIELFQLQIYIHHP
KGAKTQEKGAYESTKWRSILYNLYDLLVNEISHIGSRGKYSSGFRNIAVKENLIELMADI
CHQVFNEDTRSLEISQSYTTTQRESSDYSVPCKRKKIELGWEVIKDHLQKSQNDFDLVPW
LQIATQLISKYPASLPNCELSPLLMILSQLLPQQRHGERTPYVLRCLTEVALCQDKRSNL
ESSQKSDLLKLWNKIWCITFRGISSEQIQAENFGLLGAIIQGSLVEVDREFWKLFTGSAC
RPSCPAVCCLTLALTTSIVPGTVKMGIEQNMCEVNRSFSLKESIMKWLLFYQLEGDLENS
TEVPPILHSNFPHLVLEKILVSLTMKNCKAAMNFFQSVPECEHHQKDKEELSFSEVEELF
LQTTFDKMDFLTIVRECGIEKHQSSIGFSVHQNLKESLDRCLLGLSEQLLNNYSSEITNS
ETLVRCSRLLVGVLGCYCYMGVIAEEEAYKSELFQKAKSLMQCAGESITLFKNKTNEEFR
IGSLRNMMQLCTRCLSNCTKKSPNKIASGFFLRLLTSKLMNDIADICKSLASFIKKPFDR
GEVESMEDDTNGNLMEVEDQSSMNLFNDYPDSSVSDANEPGESQSTIGAINPLAEEYLSK
QDLLFLDMLKFLCLCVTTAQTNTVSFRAADIRRKLLMLIDSSTLEPTKSLHLHMYLMLLK
ELPGEEYPLPMEDVLELLKPLSNVCSLYRRDQDVCKTILNHVLHVVKNLGQSNMDSENTR
DAQGQFLTVIGAFWHLTKERKYIFSVRMALVNCLKTLLEADPYSKWAILNVMGKDFPVNE
VFTQFLADNHHQVRMLAAESINRLFQDTKGDSSRLLKALPLKLQQTAFENAYLKAQEGMR
EMSHSAENPETLDEIYNRKSVLLTLIAVVLSCSPICEKQALFALCKSVKENGLEPHLVKK
VLEKVSETFGYRRLEDFMASHLDYLVLEWLNLQDTEYNLSSFPFILLNYTNIEDFYRSCY
KVLIPHLVIRSHFDEVKSIANQIQEDWKSLLTDCFPKILVNILPYFAYEGTRDSGMAQQR
ETATKVYDMLKSENLLGKQIDHLFISNLPEIVVELLMTLHEPANSSASQSTDLCDFSGDL
DPAPNPPHFPSHVIKATFAYISNCHKTKLKSILEILSKSPDSYQKILLAICEQAAETNNV
YKKHRILKIYHLFVSLLLKDIKSGLGGAWAFVLRDVIYTLIHYINQRPSCIMDVSLRSFS
LCCDLLSQVCQTAVTYCKDALENHLHVIVGTLIPLVYEQVEVQKQVLDLLKYLVIDNKDN
ENLYITIKLLDPFPDHVVFKDLRITQQKIKYSRGPFSLLEEINHFLSVSVYDALPLTRLE
GLKDLRRQLELHKDQMVDIMRASQDNPQDGIMVKLVVNLLQLSKMAINHTGEKEVLEAVG
SCLGEVGPIDFSTIAIQHSKDASYTKALKLFEDKELQWTFIMLTYLNNTLVEDCVKVRSA
AVTCLKNILATKTGHSFWEIYKMTTDPMLAYLQPFRTSRKKFLEVPRFDKENPFEGLDDI
NLWIPLSENHDIWIKTLTCAFLDSGGTKCEILQLLKPMCEVKTDFCQTVLPYLIHDILLQ
DTNESWRNLLSTHVQGFFTSCLRHFSQTSRSTTPANLDSESEHFFRCCLDKKSQRTMLAV
VDYMRRQKRPSSGTIFNDAFWLDLNYLEVAKVAQSCAAHFTALLYAEIYADKKSMDDQEK
RSLAFEEGSQSTTISSLSEKSKEETGISLQDLLLEIYRSIGEPDSLYGCGGGKMLQPITR
LRTYEHEAMWGKALVTYDLETAIPSSTRQAGIIQALQNLGLCHILSVYLKGLDYENKDWC
PELEELHYQAAWRNMQWDHCTSVSKEVEGTSYHESLYNALQSLRDREFSTFYESLKYARV
KEVEEMCKRSLESVYSLYPTLSRLQAIGELESIGELFSRSVTHRQLSEVYIKWQKHSQLL
KDSDFSFQEPIMALRTVILEILMEKEMDNSQRECIKDILTKHLVELSILARTFKNTQLPE
RAIFQIKQYNSVSCGVSEWQLEEAQVFWAKKEQSLALSILKQMIKKLDASCAANNPSLKL
TYTECLRVCGNWLAETCLENPAVIMQTYLEKAVEVAGNYDGESSDELRNGKMKAFLSLAR
FSDTQYQRIENYMKSSEFENKQALLKRAKEEVGLLREHKIQTNRYTVKVQRELELDELAL
RALKEDRKRFLCKAVENYINCLLSGEEHDMWVFRLCSLWLENSGVSEVNGMMKRDGMKIP
TYKFLPLMYQLAARMGTKMMGGLGFHEVLNNLISRISMDHPHHTLFIILALANANRDEFL
TKPEVARRSRITKNVPKQSSQLDEDRTEAANRIICTIRSRRPQMVRSVEALCDAYIILAN
LDATQWKTQRKGINIPADQPITKLKNLEDVVVPTMEIKVDHTGEYGNLVTIQSFKAEFRL
AGGVNLPKIIDCVGSDGKERRQLVKGRDDLRQDAVMQQVFQMCNTLLQRNTETRKRKLTI
CTYKVVPLSQRSGVLEWCTGTVPIGEFLVNNEDGAHKRYRPNDFSAFQCQKKMMEVQKKS
FEEKYEVFMDVCQNFQPVFRYFCMEKFLDPAIWFEKRLAYTRSVATSSIVGYILGLGDRH
VQNILINEQSAELVHIDLGVAFEQGKILPTPETVPFRLTRDIVDGMGITGVEGVFRRCCE
KTMEVMRNSQETLLTIVEVLLYDPLFDWTMNPLKALYLAQRPEDETELHPTLNADDQECK
RNLSDIDQSFNKVAERVLMRLQEKLKGVEEGTVLSVGGQVNLLIQQAIDPKNLSRLFPGW
KAWV

Ligands and cofactors

IDNameFormulaCopies
ANPPhosphoaminophosphonic acid-adenylate esterC10 H17 N6 O12 P32
MGMagnesium ionMg2
ZNZinc ionZn2

Primary citation

Structural insights into the activation of ataxia-telangiectasia mutated by oxidative stress. Howes, A.C., Perisic, O., Williams, R.L. Sci Adv (2023) 9:eadi8291-eadi8291. DOI 10.1126/sciadv.adi8291 · PubMed

Other PDB entries of the same protein (UniProt P04637 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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