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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 Residues122
DetailsZN_FING: PHD-type => ECO:0000255|PROSITE-ProRule:PRU00146, ECO:0007744|PDB:4BBQ
ChainResidueDetails
ASER617-GLU678
BSER617-GLU678

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00509, ECO:0000269|Ref.28, ECO:0007744|PDB:4BBQ
ChainResidueDetails
ACYS571
BCYS574
BCYS577
BCYS582
BCYS585
BCYS588
BCYS604
BCYS609
ACYS574
ACYS577
ACYS582
ACYS585
ACYS588
ACYS604
ACYS609
BCYS571

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|Ref.28, ECO:0007744|PDB:4BBQ
ChainResidueDetails
ACYS620
BCYS623
BCYS642
BCYS645
BHIS650
BCYS653
BCYS672
BCYS675
ACYS623
ACYS642
ACYS645
AHIS650
ACYS653
ACYS672
ACYS675
BCYS620

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17525332
ChainResidueDetails
ATHR632
BTHR632

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PDB entries from 2024-09-11

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