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3HU3

Structure of p97 N-D1 R155H mutant in complex with ATPgS

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016887molecular_functionATP hydrolysis activity
B0005524molecular_functionATP binding
B0016887molecular_functionATP hydrolysis activity
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE AGS A 800
ChainResidue
AASP205
AILE380
AHIS384
AGLY408
AALA409
AMG801
AHOH802
AHOH803
AHOH804
AHOH894
AHOH953
AGLY207
AHOH955
AGLY248
ATHR249
AGLY250
ALYS251
ATHR252
ALEU253
AASN348

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 801
ChainResidue
ATHR252
AAGS800
AHOH802
AHOH803
AHOH804

site_idAC3
Number of Residues23
DetailsBINDING SITE FOR RESIDUE AGS B 800
ChainResidue
AARG359
APHE360
BASP205
BGLY207
BPRO247
BGLY248
BTHR249
BGLY250
BLYS251
BTHR252
BLEU253
BASN348
BILE380
BHIS384
BGLY408
BALA409
BMG801
BHOH802
BHOH803
BHOH804
BHOH872
BHOH909
BHOH910

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 801
ChainResidue
BTHR252
BAGS800
BHOH802
BHOH803
BHOH804

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 Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:20512113
ChainResidueDetails
APRO247
AASN348
AHIS384
BPRO247
BASN348
BHIS384

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0000269|Ref.9, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712
ChainResidueDetails
AALA2
BALA2

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER3
BSER3

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER7
ASER13
ASER462
BSER7
BSER13
BSER462

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER37
BSER37

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6,N6,N6-trimethyllysine; by VCPKMT => ECO:0000269|PubMed:22948820, ECO:0000269|PubMed:23349634
ChainResidueDetails
ALYS315
BLYS315

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976
ChainResidueDetails
ATHR436
BTHR436

site_idSWS_FT_FI8
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS8
ALYS18
BLYS8
BLYS18

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PDB entries from 2024-10-09

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