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3CRV

XPD_Helicase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0003677molecular_functionDNA binding
A0003678molecular_functionDNA helicase activity
A0003689molecular_functionDNA clamp loader activity
A0004386molecular_functionhelicase activity
A0005524molecular_functionATP binding
A0006139biological_processnucleobase-containing compound metabolic process
A0006281biological_processDNA repair
A0006338biological_processchromatin remodeling
A0009378molecular_functionfour-way junction helicase activity
A0016787molecular_functionhydrolase activity
A0016818molecular_functionhydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
A0016853molecular_functionisomerase activity
A0016887molecular_functionATP hydrolysis activity
A0032508biological_processDNA duplex unwinding
A0036121molecular_functiondouble-stranded DNA helicase activity
A0043139molecular_function5'-3' DNA helicase activity
A0046872molecular_functionmetal ion binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
A0061749molecular_functionforked DNA-dependent helicase activity
A0061775molecular_functioncohesin loader activity
A0071103biological_processDNA conformation change
A0140097molecular_functioncatalytic activity, acting on DNA
A0140584molecular_functionchromatin extrusion motor activity
A0140588biological_processchromatin looping
A0140665molecular_functionATP-dependent H3-H4 histone complex chaperone activity
A0140849molecular_functionATP-dependent H2AZ histone chaperone activity
A1990518molecular_functionsingle-stranded 3'-5' DNA helicase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FLC A 1900
ChainResidue
ALYS369
ATYR473
AGLU496
AARG531
ATRP537
AHOH717

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SF4 A 600
ChainResidue
ACYS105
ALYS108
ACYS137
ACYS88
AILE100
ACYS102

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE IPA A 1804
ChainResidue
AGLY32
ASER33
AGLY34
ALYS35
ATHR36
AHOH845

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IPA A 1806
ChainResidue
AASN21
ALYS530
AHOH826

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IPA A 1807
ChainResidue
ASER357
ATYR358
ALYS542

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IPA A 1810
ChainResidue
AHIS57
AGLY83
ATHR155

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE IPA A 1811
ChainResidue
ASER368
AILE471
AARG531
AHOH614
AHOH701

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE IPA A 1812
ChainResidue
AARG55
AALA450
AGLU451
AGLY452

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 2000
ChainResidue
AARG373
APRO401
ASER402
AGLU404
AILE405
ATYR473
AHOH680

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00541
ChainResidueDetails
AALA29

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:18510924, ECO:0007744|PDB:3CRV, ECO:0007744|PDB:5H8C
ChainResidueDetails
ACYS88
ACYS102
ACYS105
ACYS137

227344

PDB entries from 2024-11-13

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