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1E32

Structure of the N-Terminal domain and the D1 AAA domain of membrane fusion ATPase p97

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016887molecular_functionATP hydrolysis activity
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ADP A 800
ChainResidue
AASP205
AARG359
AILE380
AHIS384
AGLY408
AALA409
AHOH2031
AVAL206
AGLY207
AGLY248
ATHR249
AGLY250
ALYS251
ATHR252
ALEU253

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 Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:11163219, ECO:0000305|PubMed:14988733
ChainResidueDetails
APRO247
AHIS384

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P55072
ChainResidueDetails
AASN348

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P55072
ChainResidueDetails
AALA2

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P55072
ChainResidueDetails
ASER3
ASER7
ASER13
ASER37

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6,N6,N6-trimethyllysine; by VCPKMT => ECO:0000269|PubMed:22948820
ChainResidueDetails
ALYS315

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P55072
ChainResidueDetails
ATHR436

site_idSWS_FT_FI7
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P55072
ChainResidueDetails
ALYS8
ALYS18

237735

PDB entries from 2025-06-18

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