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6HD3

Common mode of remodeling AAA ATPases p97/CDC48 by their disassembly cofactors ASPL/PUX1

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016887molecular_functionATP hydrolysis activity
C0005524molecular_functionATP binding
C0016887molecular_functionATP hydrolysis activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue PO4 A 501
ChainResidue
AASP376
AGLU377
AARG380
AHIS407

site_idAC2
Number of Residues5
Detailsbinding site for residue PO4 A 502
ChainResidue
ALYS67
AARG97
AASP197
CLYS67
CARG68

site_idAC3
Number of Residues5
Detailsbinding site for residue PO4 A 503
ChainResidue
ALYS239
ALEU338
ALYS339
ASER340
AHOH609

site_idAC4
Number of Residues15
Detailsbinding site for residue ADP A 504
ChainResidue
AASP208
AGLY210
APRO250
AGLY251
ASER252
AGLY253
ALYS254
ATHR255
ALEU256
AARG362
AVAL383
AHIS387
AGLY411
AALA412
AHOH618

site_idAC5
Number of Residues12
Detailsbinding site for residue ADP C 801
ChainResidue
CASP208
CGLY210
CGLY251
CSER252
CGLY253
CLYS254
CTHR255
CLEU256
CARG362
CHIS387
CGLY411
CALA412

Functional Information from PROSITE/UniProt
site_idPS00674
Number of Residues19
DetailsAAA AAA-protein family signature. ViVMgATNrpnsIDpALr.R
ChainResidueDetails
AVAL344-ARG362

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|Ref.15, ECO:0007744|PDB:6HD3
ChainResidueDetails
AGLY210
AGLY248
AHIS387
CGLY210
CGLY248
CHIS387

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:22223895
ChainResidueDetails
ASER2
CSER2

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:17693538
ChainResidueDetails
ASER41
CSER41

224572

PDB entries from 2024-09-04

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