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4EYU

The free structure of the mouse C-terminal domain of KDM6B

Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0046872molecular_functionmetal ion binding
A0071557biological_processhistone H3-K27 demethylation
A0071558molecular_functionhistone H3-tri/di-methyl-lysine-27 demethylase activity
B0005634cellular_componentnucleus
B0046872molecular_functionmetal ion binding
B0071557biological_processhistone H3-K27 demethylation
B0071558molecular_functionhistone H3-tri/di-methyl-lysine-27 demethylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE OGA A 1700
ChainResidue
ALYS1381
AHOH1827
ATHR1387
AHIS1390
AGLU1392
ASER1398
AASN1400
AHIS1470
ANI1701
AHOH1801

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NI A 1701
ChainResidue
AHIS1390
AGLU1392
AHIS1470
AOGA1700
AHOH1827

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1702
ChainResidue
ACYS1575
ACYS1578
ACYS1602
ACYS1605

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE OGA B 1700
ChainResidue
BLYS1381
BTHR1387
BHIS1390
BGLU1392
BSER1398
BASN1400
BHIS1470
BNI1701
BHOH1807
BHOH1832

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NI B 1701
ChainResidue
BHIS1390
BGLU1392
BHIS1470
BOGA1700
BHOH1832

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1702
ChainResidue
BCYS1575
BCYS1578
BCYS1602
BCYS1605

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues326
DetailsDomain: {"description":"JmjC","evidences":[{"source":"PROSITE-ProRule","id":"PRU00538","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"O14607","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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