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1S3S

Crystal structure of AAA ATPase p97/VCP ND1 in complex with p47 C

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016887molecular_functionATP hydrolysis activity
B0005524molecular_functionATP binding
B0016887molecular_functionATP hydrolysis activity
C0005524molecular_functionATP binding
C0016887molecular_functionATP hydrolysis activity
D0005524molecular_functionATP binding
D0016887molecular_functionATP hydrolysis activity
E0005524molecular_functionATP binding
E0016887molecular_functionATP hydrolysis activity
F0005524molecular_functionATP binding
F0016887molecular_functionATP hydrolysis activity
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADP A 800
ChainResidue
AASP205
AHIS384
AGLY408
AALA409
AHOH808
AGLY207
AGLY248
ATHR249
AGLY250
ALYS251
ATHR252
ALEU253
AILE380

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ADP B 801
ChainResidue
BASP205
BVAL206
BGLY207
BGLY248
BTHR249
BGLY250
BLYS251
BTHR252
BLEU253
BILE380
BHIS384
BGLY408
BALA409
FARG359

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ADP C 802
ChainResidue
CASP205
CVAL206
CGLY207
CGLY248
CTHR249
CGLY250
CLYS251
CTHR252
CLEU253
CILE380
CHIS384
CGLY408
CALA409
CHOH803
DARG359

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ADP D 803
ChainResidue
DASP205
DGLY207
DGLY248
DTHR249
DGLY250
DLYS251
DTHR252
DLEU253
DHIS384
DGLY408
DALA409
DALA412

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADP E 804
ChainResidue
CARG359
EASP205
EGLY207
EGLY248
ETHR249
EGLY250
ELYS251
ETHR252
ELEU253
EILE380
EHIS384
EGLY408
EALA409

site_idAC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADP F 805
ChainResidue
FASP205
FGLY207
FGLY248
FTHR249
FGLY250
FLYS251
FTHR252
FLEU253
FILE380
FHIS384
FGLY408
FALA409
FHOH810

Functional Information from PROSITE/UniProt
site_idPS00674
Number of Residues19
DetailsAAA AAA-protein family signature. ViVMaATNrpnsIDpALr.R
ChainResidueDetails
AVAL341-ARG359

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues42
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11163219","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"14988733","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P55072","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P55072","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsModified residue: {"description":"N6,N6,N6-trimethyllysine; by VCPKMT","evidences":[{"source":"PubMed","id":"22948820","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P55072","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P55072","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues154
DetailsDomain: {"description":"UBX","evidences":[{"source":"PROSITE-ProRule","id":"PRU00215","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9UNZ2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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