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2V1X

Crystal structure of human RECQ-like DNA helicase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0004386molecular_functionhelicase activity
A0005524molecular_functionATP binding
A0006310biological_processDNA recombination
B0003676molecular_functionnucleic acid binding
B0004386molecular_functionhelicase activity
B0005524molecular_functionATP binding
B0006310biological_processDNA recombination
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1594
ChainResidue
ASER120
AADP1593
AHOH2018
AHOH2033
AHOH2034
AHOH2144

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1595
ChainResidue
ACYS478
ACYS453
ACYS471
ACYS475

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1596
ChainResidue
AHIS357
AASP379
ALYS380

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 1597
ChainResidue
AGLU485

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 1598
ChainResidue
ATHR115
ATYR399

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1599
ChainResidue
AARG486
AGLN589
AHOH2037

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 1594
ChainResidue
BADP1593
BHOH2027
BHOH2037
BHOH2038
BHOH2162
BHOH2165

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1595
ChainResidue
BCYS453
BCYS471
BCYS475
BCYS478

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 1596
ChainResidue
BGLN324
BALA346
BTHR371

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 1597
ChainResidue
BGLN324

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 1598
ChainResidue
BHIS357
BILE378
BASP379
BLYS380

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 1599
ChainResidue
BTHR115
BTYR399

site_idBC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 1600
ChainResidue
BGLN589

site_idBC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ADP A 1593
ChainResidue
ALEU89
ALYS91
AARG93
AGLN96
APRO114
ATHR115
AGLY116
AGLY117
AGLY118
ALYS119
ASER120
AASP379
AMG1594
AHOH2011
AHOH2018
AHOH2033
AHOH2144
AHOH2145
AHOH2146

site_idBC6
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ADP B 1593
ChainResidue
BLEU89
BLYS91
BARG93
BGLN96
BTHR115
BGLY116
BGLY117
BGLY118
BLYS119
BSER120
BASP379
BMG1594
BHOH2027
BHOH2160
BHOH2161
BHOH2162
BHOH2163
BHOH2164
BHOH2165
BHOH2166

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 1601
ChainResidue
BGLN292
BTYR418
BPHE420
BGLU540
BGLU543
BHOH2167

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 1602
ChainResidue
BPHE424
BSER428
BILE567
BSER568
BHOH2169

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:19151156
ChainResidueDetails
ALYS119
BLYS119

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000305|PubMed:19151156, ECO:0007744|PDB:2V1X
ChainResidueDetails
ALYS91
BGLN96
BGLY116
BGLY118
BLYS119
BSER120
AARG93
AGLN96
AGLY116
AGLY118
ALYS119
ASER120
BLYS91
BARG93

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:19151156, ECO:0000269|PubMed:25831490, ECO:0007744|PDB:2V1X, ECO:0007744|PDB:2WWY, ECO:0007744|PDB:4U7D
ChainResidueDetails
ACYS453
ACYS471
ACYS475
ACYS478
BCYS453
BCYS471
BCYS475
BCYS478

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS514
ALYS522
BLYS514
BLYS522

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER597
BSER597

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q6AYJ1
ChainResidueDetails
ASER602
BSER602

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PDB entries from 2025-06-11

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