Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6P4F

Crystal structure of the XPB-Bax1-forked DNA ternary complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0004386molecular_functionhelicase activity
A0005524molecular_functionATP binding
A0006281biological_processDNA repair
A0006367biological_processtranscription initiation at RNA polymerase II promoter
A0016787molecular_functionhydrolase activity
A0016853molecular_functionisomerase activity
A0032508biological_processDNA duplex unwinding
A0043138molecular_function3'-5' DNA helicase activity
A0097550cellular_componenttranscription preinitiation complex
C0003677molecular_functionDNA binding
C0004386molecular_functionhelicase activity
C0005524molecular_functionATP binding
C0006281biological_processDNA repair
C0006367biological_processtranscription initiation at RNA polymerase II promoter
C0016787molecular_functionhydrolase activity
C0016853molecular_functionisomerase activity
C0032508biological_processDNA duplex unwinding
C0043138molecular_function3'-5' DNA helicase activity
C0097550cellular_componenttranscription preinitiation complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue MG A 501
ChainResidue
AASP155
BPO4401
EDA8
FDG19

site_idAC2
Number of Residues2
Detailsbinding site for residue MG A 503
ChainResidue
ASER245
ALEU246

site_idAC3
Number of Residues4
Detailsbinding site for residue MG A 506
ChainResidue
ALEU281
ALEU272
ALEU275
AASP277

site_idAC4
Number of Residues1
Detailsbinding site for residue CL A 509
ChainResidue
AASP133

site_idAC5
Number of Residues5
Detailsbinding site for residue PO4 B 401
ChainResidue
AMG501
BGLU204
EDC7
FDG19
FDA20

site_idAC6
Number of Residues1
Detailsbinding site for residue MG B 404
ChainResidue
BGLU139

site_idAC7
Number of Residues1
Detailsbinding site for residue CL B 408
ChainResidue
BGLU102

site_idAC8
Number of Residues1
Detailsbinding site for residue CL B 410
ChainResidue
BGLY277

site_idAC9
Number of Residues1
Detailsbinding site for residue CL B 412
ChainResidue
BLEU17

site_idAD1
Number of Residues4
Detailsbinding site for residue MG C 504
ChainResidue
CPHE330
CSER376
CPHE403
CLEU407

site_idAD2
Number of Residues4
Detailsbinding site for residue MG C 505
ChainResidue
CLEU275
CASP277
CPHE278
CLEU281

site_idAD3
Number of Residues3
Detailsbinding site for residue PO4 D 401
ChainResidue
DGLU5
GDC10
HDG16

site_idAD4
Number of Residues1
Detailsbinding site for residue MG D 404
ChainResidue
DLEU287

site_idAD5
Number of Residues1
Detailsbinding site for residue MG E 102
ChainResidue
EDA11

site_idAD6
Number of Residues4
Detailsbinding site for residue PO4 F 101
ChainResidue
BGLU5
EDC10
FDT15
FDG16

site_idAD7
Number of Residues2
Detailsbinding site for residue CL G 101
ChainResidue
GDA11
GDT12

site_idAD8
Number of Residues1
Detailsbinding site for residue MG H 101
ChainResidue
HDA20

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O29890
ChainResidueDetails
BGLU265
BASP297
BGLU310
DGLU265
DASP297
DGLU310

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:32986831
ChainResidueDetails
AARG127
CARG127

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Wedge residue => ECO:0000269|PubMed:32986831
ChainResidueDetails
APHE278
CPHE278

222036

PDB entries from 2024-07-03

PDB statisticsPDBj update infoContact PDBjnumon