4Q5V: DNA polymerase alpha catalytic subunit

Crystal structure of the catalytic core of human DNA polymerase alpha in ternary complex with an RNA-primed DNA template and aphidicolin. Determined by X-ray diffraction at 2.52 Å resolution. Released 26 Nov 2014.

Method
X-ray diffraction
Resolution
2.52 Å
Organism
Homo sapiens
Chains
6
Atoms
15,085
Mol. weight
231.73 kDa
Ligands
2ZE
Released
26 Nov 2014

Explore 4Q5V in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4Q5V contains 89 α-helices and 75 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: 46 helices, 37 β-strands

ElementResiduesLengthSheet
β-strand340-350111
β-strand359-36791
α-helix368-3703
β-strand372-38091
β-strand385-39172
β-strand394-39633
β-strand403-40753
α-helix410-4167
α-helix417-4215
α-helix422-4254
β-strand431-43882
β-strand449-45792
α-helix463-4653
β-strand473-47752
α-helix483-4908
β-strand497-50261
β-strand50511
β-strand51214
β-strand516-52051
α-helix523-5253
β-strand526-52941
α-helix533-5364
β-strand537-548125
β-strand555-568145
α-helix573-5753
β-strand581-58665
α-helix594-5952
α-helix598-6058
β-strand609-61135
α-helix615-62915
β-strand633-63645
α-helix639-6435
α-helix644-65310
α-helix659-6624
β-strand66514
α-helix679-6846
β-strand689-69245
α-helix693-7008
α-helix708-7114
α-helix712-7165
α-helix725-7317
α-helix735-75824
α-helix761-77212
α-helix776-7794
α-helix784-79815
β-strand80112
α-helix804-8074
α-helix835-8373
β-strand84416
α-helix845-8473
β-strand850-85237
β-strand856-86167
α-helix864-8718
α-helix898-9036
α-helix907-9093
α-helix910-92920
α-helix938-96023
α-helix970-99223
β-strand997-100047
β-strand100216
β-strand1005-100957
α-helix1015-103016
β-strand1038-1051147
β-strand1054-106297
β-strand1068-107587
α-helix1078-10803
α-helix1086-110015
α-helix1105-112521
β-strand1135-113848
α-helix1143-11453
α-helix1149-11513
α-helix1153-116412
β-strand1174-117748
β-strand1178-117929
β-strand1180110
α-helix1188-11903
β-strand1192-119329
α-helix1195-12006
β-strand1206110
α-helix1208-12103
α-helix1211-12166
α-helix1217-12248
α-helix1232-12387
Chain E: 43 helices, 38 β-strands
ElementResiduesLengthSheet
β-strand340-3491011
β-strand359-367911
α-helix368-3703
β-strand372-380911
β-strand385-391712
β-strand394-397413
β-strand402-407613
α-helix410-4167
α-helix417-4215
α-helix422-4254
β-strand431-436612
β-strand438114
β-strand451-457712
β-strand473-477512
α-helix483-4919
β-strand497-502611
β-strand505111
β-strand512115
β-strand516-520511
α-helix523-5253
β-strand526-529411
α-helix533-5364
β-strand537-5481216
β-strand555-5681416
α-helix573-5753
β-strand581-586616
α-helix594-5952
α-helix598-6058
β-strand609-611316
α-helix615-62915
β-strand633-636416
α-helix639-6435
α-helix644-65310
α-helix659-6624
β-strand665115
α-helix679-6846
β-strand689-692416
α-helix693-7008
α-helix708-7114
α-helix712-7165
α-helix725-7306
α-helix735-75824
α-helix761-77212
α-helix776-7805
α-helix785-79814
β-strand801114
α-helix802-8076
β-strand844117
α-helix845-8473
β-strand850-852318
β-strand856-861618
α-helix864-8718
α-helix900-9034
α-helix907-9093
α-helix910-92920
α-helix938-96023
α-helix970-99223
β-strand997-1000418
β-strand1002117
β-strand1005-1009518
α-helix1015-102915
β-strand1038-10511418
β-strand1054-1062918
β-strand1068-1075818
α-helix1078-10803
α-helix1086-110015
α-helix1105-112521
β-strand1135-1138419
α-helix1149-11513
α-helix1153-116412
β-strand1174-1177419
β-strand1178-1179220
β-strand1180121
α-helix1188-11903
β-strand1192-1193220
α-helix1195-12006
β-strand1206121
α-helix1208-12103
α-helix1211-12166
α-helix1217-12248
α-helix1232-12387

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
DNA polymerase alpha catalytic subunitA, Eprotein922Homo sapiensP09884 (AlphaFold model)
RNA primerB, FRNA11
DNA templateC, GDNA21
Sequence of entity 1 (A, E), FASTA
>4Q5V_1 DNA polymerase alpha catalytic subunit (chains A, E)
DEEQVFHFYWLDAYEDQYNQPGVVFLFGKVWIESAETHVSCCVMVKNIERTLYFLPREMK
IDLNTGKETGTPISMKDVYEEFDEKIATKYKIMKFKSKPVEKNYAFEIPDVPEKSEYLEV
KYSAEMPQLPQDLKGETFSHVFGTNTSSLELFLMNRKIKGPCWLEVKSPQLLNQPVSWCK
AEAMALKPDLVNVIKDVSPPPLVVMAFSMKTMQNAKNHQNEIIAMAALVHHSFALDKAAP
KPPFQSHFCVVSKPKDCIFPYAFKEVIEKKNVKVEVAATERTLLGFFLAKVHKIDPDIIV
GHNIYGFELEVLLQRINVCKAPHWSKIGRLKRSNMPKLGGRSGFGERNATCGRMICDVEI
SAKELIRCKSYHLSELVQQILKTERVVIPMENIQNMYSESSQLLYLLEHTWKDAKFILQI
MCELNVLPLALQITNIAGNIMSRTLMGGRSERNEFLLLHAFYENNYIVPDKQIFRKPQQK
LGDEDEEIDGDTNKYKKGRKKAAYAGGLVLDPKVGFYDKFILLLDFNSLYPSIIQEFNIC
FTTVQRVASEAQKVTEDGEQEQIPELPDPSLEMGILPREIRKLVERRKQVKQLMKQQDLN
PDLILQYDIRQKALKLTANSMYGCLGFSYSRFYAKPLAALVTYKGREILMHTKEMVQKMN
LEVIYGDTDSIMINTNSTNLEEVFKLGNKVKSEVNKLYKLLEIDIDGVFKSLLLLKKKKY
AALVVEPTSDGNYVTKQELKGLDIVRRDWCDLAKDTGNFVIGQILSDQSRDTIVENIQKR
LIEIGENVLNGSVPVSQFEINKALTKDPQDYPDKKSLPHVHVALWINSQGGRKVKAGDTV
SYVICQDGSNLTASQRAYAPEQLQKQDNLTIDTQYYLAQQIHPVVARICEPIDGIDAVLI
ATWLGLDPTQFRVHHYHKDEEN
Sequence of entity 2 (B, F), FASTA
>4Q5V_2 RNA primer (chains B, F)
GCCUGGAGCGC
Sequence of entity 3 (C, G), FASTA
>4Q5V_3 DNA template (chains C, G)
ATTACTATAGGCGCTCCAGGC

Ligands and cofactors

IDNameFormulaCopies
2ZE(3R,4R,4aR,6aS,8R,9R,11aS,11bS)-4,9-bis(hydroxymethyl)-4,11b-dimethyltetradecah…C20 H34 O42

Primary citation

Structural basis for inhibition of DNA replication by aphidicolin. Baranovskiy, A.G., Babayeva, N.D., Suwa, Y. et al. Nucleic Acids Res (2014) 42:14013-14021. DOI 10.1093/nar/gku1209 · PubMed

Other PDB entries of the same protein (UniProt P09884 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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