2Q71

Uroporphyrinogen Decarboxylase G168R single mutant enzyme in complex with coproporphyrinogen-III

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004853	molecular_function	uroporphyrinogen decarboxylase activity
A	0005515	molecular_function	protein binding
A	0005654	cellular_component	nucleoplasm
A	0005829	cellular_component	cytosol
A	0006778	biological_process	porphyrin-containing compound metabolic process
A	0006779	biological_process	porphyrin-containing compound biosynthetic process
A	0006782	biological_process	protoporphyrinogen IX biosynthetic process
A	0006783	biological_process	heme biosynthetic process
A	0006784	biological_process	heme A biosynthetic process
A	0006785	biological_process	heme B biosynthetic process
A	0006787	biological_process	porphyrin-containing compound catabolic process
A	0016829	molecular_function	lyase activity
A	0016831	molecular_function	carboxy-lyase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	26
Details	BINDING SITE FOR RESIDUE CP3 A 867

Chain	Residue
A	ARG37
A	PHE84
A	SER85
A	ASP86
A	ILE87
A	MET100
A	PRO106
A	PHE154
A	TYR164
A	PHE217
A	SER219
A	GLN38
A	HIS339
A	HOH1143
A	HOH1306
A	HOH1326
A	HOH1328
A	HOH1350
A	HOH1374
A	ALA39
A	GLY40
A	ARG41
A	PHE46
A	PHE55
A	ILE82
A	ILE83

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Functional Information from PROSITE/UniProt

site_id	PS00906
Number of Residues	10
Details	UROD_1 Uroporphyrinogen decarboxylase signature 1. PVWCMRQAGR

Chain	Residue	Details
A	PRO32-ARG41

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14633982","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1R3W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1R3Y","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14633982","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1R3T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1R3W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1R3Y","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14633982","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1R3Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1R3S","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14633982","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1R3Y","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14633982","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1R3T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1R3W","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	1
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"14633982","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1uro

Chain	Residue	Details
A	TYR164
A	ASP86

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site_id	MCSA1
Number of Residues	5
Details	M-CSA 914

Chain	Residue	Details
A	ARG37	proton shuttle (general acid/base)
A	ARG41	electrostatic stabiliser
A	ARG50	proton shuttle (general acid/base)
A	ASP86	enhance reactivity, modifies pKa, transition state stabiliser
A	TYR164	electrostatic stabiliser

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