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2AEX

The 1.58A Crystal Structure of Human Coproporphyrinogen Oxidase Reveals the Structural Basis of Hereditary Coproporphyria

Functional Information from GO Data
ChainGOidnamespacecontents
A0004109molecular_functioncoproporphyrinogen oxidase activity
A0006779biological_processporphyrin-containing compound biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE CIT A 500
ChainResidue
ASER244
AHOH635
AHOH636
AHOH640
AHOH641
AHOH663
AHOH664
AHOH844
AHIS258
AASN260
AARG262
AGLY406
AGLY411
ASER412
AARG413
ASER416

Functional Information from PROSITE/UniProt
site_idPS01021
Number of Residues25
DetailsCOPROGEN_OXIDASE Coproporphyrinogen III oxidase signature. KkWCddYFfIaHRgErRGIGGIFFD
ChainResidueDetails
ALYS316-ASP340

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues45
DetailsRegion: {"description":"Important for dimerization","evidences":[{"source":"PubMed","id":"16176984","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"16176984","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16176984","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2AEX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Important for dimerization","evidences":[{"source":"PubMed","id":"16176984","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P36552","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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