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1WES

Solution structure of PHD domain in inhibitor of growth family, member 1-like

Functional Information from GO Data
ChainGOidnamespacecontents
A0003682molecular_functionchromatin binding
A0005634cellular_componentnucleus
A0006325biological_processchromatin organization
A0008285biological_processnegative regulation of cell population proliferation
A0042981biological_processregulation of apoptotic process
A2000772biological_processregulation of cellular senescence
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 201
ChainResidue
ACYS19
ACYS21
AHIS43
ACYS46

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
ACYS32
ACYS37
ACYS59
ACYS62

Functional Information from PROSITE/UniProt
site_idPS01359
Number of Residues44
DetailsZF_PHD_1 Zinc finger PHD-type signature. Cl.Cnqvsygem.....................................IgCdneqCpiewFHfsCvsltykpkgk...................................WyCpkC
ChainResidueDetails
ACYS19-CYS62

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues49
DetailsZinc finger: {"description":"PHD-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00146","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q9UK53","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsSite: {"description":"Histone H3K4me3 binding","evidences":[{"source":"UniProtKB","id":"Q9UK53","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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