2AEX

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004109	molecular_function	coproporphyrinogen oxidase activity
A	0006779	biological_process	porphyrin-containing compound biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE CIT A 500

Chain	Residue
A	SER244
A	HOH635
A	HOH636
A	HOH640
A	HOH641
A	HOH663
A	HOH664
A	HOH844
A	HIS258
A	ASN260
A	ARG262
A	GLY406
A	GLY411
A	SER412
A	ARG413
A	SER416

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Functional Information from PROSITE/UniProt

site_id	PS01021
Number of Residues	25
Details	COPROGEN_OXIDASE Coproporphyrinogen III oxidase signature. KkWCddYFfIaHRgErRGIGGIFFD

Chain	Residue	Details
A	LYS316-ASP340

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:16176984

Chain	Residue	Details
A	PHE259

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	SER245

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING:

Chain	Residue	Details
A	TYR261
A	SER412

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site_id	SWS_FT_FI4
Number of Residues	1
Details	SITE: Important for dimerization

Chain	Residue	Details
A	ARG328

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q3B7D0

Chain	Residue	Details
A	LEU113

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P36552

Chain	Residue	Details
A	PHE405

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