3GQC: Human Rev1-DNA-dNTP ternary complex

Structure of human Rev1-DNA-dNTP ternary complex. Determined by X-ray diffraction at 2.5 Å resolution. Released 19 May 2009.

Method
X-ray diffraction
Resolution
2.5 Å
Organism
Homo sapiens
Chains
12
Atoms
15,522
Mol. weight
260.17 kDa
Ligands
DCP, MG
Released
19 May 2009

Explore 3GQC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3GQC contains 102 α-helices and 74 β-strands across 4 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: 28 helices, 20 β-strands

ElementResiduesLengthSheet
α-helix345-35511
α-helix357-37519
α-helix384-3874
β-strand419-42461
α-helix427-4326
β-strand444-44632
β-strand45413
β-strand46114
α-helix463-4697
α-helix470-4745
α-helix500-5023
β-strand50313
α-helix5061
β-strand50715
α-helix5081
β-strand510-51122
α-helix513-5164
β-strand52515
α-helix526-5327
α-helix5361
β-strand537-53932
α-helix543-55816
β-strand564-56851
β-strand571-57551
α-helix577-5837
α-helix587-60216
β-strand606-61161
α-helix614-62411
β-strand629-63131
α-helix634-6363
α-helix637-6437
β-strand64516
α-helix646-6483
α-helix654-6629
β-strand66716
α-helix668-6714
α-helix676-6838
α-helix685-69410
α-helix701-7033
β-strand712-71657
α-helix725-74521
β-strand748-760137
α-helix7611
β-strand76714
β-strand777-790147
α-helix793-80513
α-helix811-8133
β-strand814-826137
Chain B: 26 helices, 18 β-strands
ElementResiduesLengthSheet
α-helix345-35511
α-helix357-37620
α-helix384-3896
β-strand419-42468
α-helix427-4326
β-strand444-44639
β-strand454110
α-helix463-4708
α-helix500-5023
β-strand503110
α-helix5061
β-strand507111
α-helix5081
β-strand510-51129
α-helix513-5164
β-strand525111
α-helix526-5327
α-helix5361
β-strand537-53939
α-helix543-55816
β-strand564-56858
β-strand571-57558
α-helix577-5815
α-helix587-60216
β-strand606-61168
α-helix614-62411
β-strand629-63138
α-helix634-64310
β-strand645112
α-helix646-6483
α-helix654-6618
β-strand667112
α-helix668-6714
α-helix676-6838
α-helix685-69410
α-helix701-7033
β-strand712-716513
α-helix725-74622
β-strand748-7601313
α-helix7611
β-strand777-7901413
α-helix793-80513
α-helix811-8133
β-strand814-8261313
Chain C: 24 helices, 18 β-strands
ElementResiduesLengthSheet
α-helix345-35511
α-helix357-37620
β-strand419-424614
α-helix427-4326
α-helix437-4393
β-strand444-446315
β-strand454116
α-helix463-4719
β-strand503116
α-helix5061
β-strand507117
α-helix5081
β-strand510-511215
α-helix513-5175
β-strand525117
α-helix526-5327
α-helix5361
β-strand537-539315
α-helix543-55816
β-strand564-568514
β-strand571-575514
α-helix577-5815
α-helix587-60216
β-strand606-611614
α-helix614-62411
β-strand629-631314
α-helix637-6426
β-strand645118
α-helix646-6483
α-helix654-6618
β-strand667118
α-helix668-6714
α-helix676-6838
α-helix685-69410
α-helix701-7033
β-strand712-716519
α-helix725-74521
β-strand748-7601319
β-strand777-7901419
α-helix793-80513
α-helix811-8133
β-strand814-8261319
Chain D: 24 helices, 18 β-strands
ElementResiduesLengthSheet
α-helix347-3559
α-helix357-37620
α-helix384-3885
β-strand419-424620
α-helix427-4326
β-strand444-446321
β-strand454122
α-helix463-4708
α-helix497-5004
β-strand503122
α-helix5061
β-strand507123
α-helix5081
β-strand510-511221
α-helix513-5164
β-strand525123
α-helix526-5327
β-strand537-539321
α-helix543-55715
β-strand564-568520
β-strand571-575520
α-helix577-5837
α-helix587-60216
β-strand606-611620
α-helix614-62411
β-strand629-631320
α-helix634-6429
β-strand645124
α-helix646-6483
α-helix654-6618
β-strand667124
α-helix668-6714
α-helix676-6838
α-helix685-69410
β-strand712-716525
α-helix725-74622
β-strand748-7601325
α-helix7611
β-strand777-7901425
α-helix793-80513
α-helix811-8133
β-strand814-8261325

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
DNA repair protein REV1A, B, C, Dprotein504Homo sapiensQ9UBZ9 (AlphaFold model)
5'-d(*ap*tp*cp*cp*tp*cp*cp*cp*cp*tp*ap*(doc))-3'E, G, I, KDNA12
5'-d(*tp*ap*ap*gp*gp*tp*ap*gp*gp*gp*gp*ap*gp*gp*ap*t)-3'F, H, J, LDNA16
Sequence of entity 1 (A, B, C, D), FASTA
>3GQC_1 DNA repair protein REV1 (chains A, B, C, D)
STFSKAAPSVPSKPSDCNFISNFYSHSRLHHISMWKCELTEFVNTLQRQSNGIFPGREKL
KKMKTGRSALVVTDTGDMSVLNSPRHQSCIMHVDMDCFFVSVGIRNRPDLKGKPVAVTSN
RGTGRAPLRPGANPQLEWQYYQNKILKGKAADIPDSSLWENPDSAQANGIDSVLSRAEIA
SCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSC
DEALVDITEILAETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQ
YHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGPKTGQ
MLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMK
GKRLTLKIMVRKPGAPVETAKFGGHGICDNIARTVTLDQATDNAKIIGKAMLNMFHTMKL
NISDMRGVGIHVNQLVPTNLNPST
Sequence of entity 2 (E, G, I, K), FASTA
>3GQC_2 5'-D(*AP*TP*CP*CP*TP*CP*CP*CP*CP*TP*AP*(DOC))-3' (chains E, G, I, K)
ATCCTCCCCTAC
Sequence of entity 3 (F, H, J, L), FASTA
>3GQC_3 5'-D(*TP*AP*AP*GP*GP*TP*AP*GP*GP*GP*GP*AP*GP*GP*AP*T)-3' (chains F, H, J, L)
TAAGGTAGGGGAGGAT

Ligands and cofactors

IDNameFormulaCopies
DCP2'-deoxycytidine-5'-triphosphateC9 H16 N3 O13 P34
MGMagnesium ionMg13

Primary citation

Structure of the human Rev1-DNA-dNTP ternary complex. Swan, M.K., Johnson, R.E., Prakash, L. et al. J Mol Biol (2009) 390:699-709. DOI 10.1016/j.jmb.2009.05.026 · PubMed

Other PDB entries of the same protein (UniProt Q9UBZ9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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