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8HL7

Crystal structure of p97 N/D1 in complex with a valosin-containing protein methyltransferase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006338biological_processchromatin remodeling
A0008168molecular_functionmethyltransferase activity
A0008276molecular_functionprotein methyltransferase activity
A0016279molecular_functionprotein-lysine N-methyltransferase activity
A0018022biological_processpeptidyl-lysine methylation
A0018023biological_processpeptidyl-lysine trimethylation
A0032259biological_processmethylation
A0032780biological_processnegative regulation of ATP-dependent activity
A0032991cellular_componentprotein-containing complex
A0042054molecular_functionhistone methyltransferase activity
A0051117molecular_functionATPase binding
B0005524molecular_functionATP binding
B0016887molecular_functionATP hydrolysis activity
Functional Information from PROSITE/UniProt
site_idPS00674
Number of Residues19
DetailsAAA AAA-protein family signature. ViVMaATNrpnsIDpALr.R
ChainResidueDetails
BVAL341-ARG359

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:20512113
ChainResidueDetails
BPRO247
BASN348
BHIS384
ATRP126
AALA143
ATYR148

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
BSER37

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6,N6,N6-trimethyllysine; by VCPKMT => ECO:0000269|PubMed:22948820, ECO:0000269|PubMed:23349634
ChainResidueDetails
BM3L315

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976
ChainResidueDetails
BTHR436

224931

PDB entries from 2024-09-11

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