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4BBQ

Crystal structure of the CXXC and PHD domain of Human Lysine-specific Demethylase 2A (KDM2A)(FBXL11)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0008270molecular_functionzinc ion binding
B0003677molecular_functionDNA binding
B0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1677
ChainResidue
AASP657
AGLY658
AHOH2049
BLYS601
BGLN602
BHOH2006
BHOH2029

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1677
ChainResidue
BCYS588
BCYS604
BCYS582
BCYS585

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1678
ChainResidue
ACYS582
ACYS585
ACYS588
ACYS604

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1679
ChainResidue
ACYS571
ACYS574
ACYS577
ACYS609

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1678
ChainResidue
BCYS571
BCYS574
BCYS577
BCYS609

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1680
ChainResidue
ACYS642
ACYS645
ACYS672
ACYS675

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1681
ChainResidue
ACYS620
ACYS623
AHIS650
ACYS653

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1679
ChainResidue
BCYS642
BCYS645
BCYS672
BCYS675

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1680
ChainResidue
BCYS620
BCYS623
BHIS650
BCYS653

Functional Information from PROSITE/UniProt
site_idPS00197
Number of Residues9
Details2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CVQGECGVC
ChainResidueDetails
ACYS577-CYS585

site_idPS01359
Number of Residues56
DetailsZF_PHD_1 Zinc finger PHD-type signature. CslCgevdqneetqdfekklm............................EcCi...Cnei.VHpgClqmdgegllneelpnc.............................WeCpkC
ChainResidueDetails
ACYS620-CYS675

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00509","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2012","submissionDatabase":"PDB data bank","title":"Crystal Structure of the Cxxc and Phd Domain of Human Lysine-Specific Demethylase 2A (Kdm2A)(Fbxl11).","authors":["Allerston C.K.","Watson A.A.","Edlich C.","Li B.","Chen Y.","Ball L.","Krojer T.","Arrowsmith C.H.","Edwards A.","Bountra C.","von Delft F.","Laue E.D.","Gileadi O."]}},{"source":"PDB","id":"4BBQ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2012","submissionDatabase":"PDB data bank","title":"Crystal Structure of the Cxxc and Phd Domain of Human Lysine-Specific Demethylase 2A (Kdm2A)(Fbxl11).","authors":["Allerston C.K.","Watson A.A.","Edlich C.","Li B.","Chen Y.","Ball L.","Krojer T.","Arrowsmith C.H.","Edwards A.","Bountra C.","von Delft F.","Laue E.D.","Gileadi O."]}},{"source":"PDB","id":"4BBQ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17525332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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