1R3V

Uroporphyrinogen Decarboxylase single mutant D86E in complex with coproporphyrinogen-I

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	0005737	cellular_component	cytoplasm
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
A	0042168	biological_process	heme metabolic process
A	0048034	biological_process	heme O biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	31
Details	BINDING SITE FOR RESIDUE 1CP A 368

Chain	Residue
A	ARG37
A	MET100
A	PRO106
A	PHE154
A	TYR164
A	GLY170
A	PHE217
A	SER219
A	HIS339
A	BME9500
A	HOH9548
A	ALA39
A	HOH9612
A	HOH9617
A	HOH9628
A	HOH9663
A	HOH9693
A	HOH9731
A	HOH9771
A	HOH9783
A	HOH9788
A	HOH9823
A	ARG41
A	HOH9838
A	HOH9859
A	PHE46
A	PHE55
A	PHE84
A	SER85
A	GLU86
A	ILE87

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE BME A 9500

Chain	Residue
A	ARG37
A	1CP368
A	HOH9881
A	HOH9882

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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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site_id	PS00907
Number of Residues	17
Details	UROD_2 Uroporphyrinogen decarboxylase signature 2. IGFAGaPWTLmtYmv.EG

Chain	Residue	Details
A	ILE152-GLY168

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:14633982, ECO:0007744|PDB:1R3W, ECO:0007744|PDB:1R3Y

Chain	Residue	Details
A	ARG37
A	GLU86
A	HIS339

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:14633982, ECO:0007744|PDB:1R3T, ECO:0007744|PDB:1R3W, ECO:0007744|PDB:1R3Y

Chain	Residue	Details
A	ALA39
A	ARG41

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:14633982, ECO:0007744|PDB:1R3Q, ECO:0007744|PDB:1R3S

Chain	Residue	Details
A	ARG50

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site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:14633982, ECO:0007744|PDB:1R3Y

Chain	Residue	Details
A	TYR164

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site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:14633982, ECO:0007744|PDB:1R3T, ECO:0007744|PDB:1R3W

Chain	Residue	Details
A	SER219

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site_id	SWS_FT_FI6
Number of Residues	1
Details	SITE: Transition state stabilizer => ECO:0000269|PubMed:14633982

Chain	Residue	Details
A	GLU86

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378

Chain	Residue	Details
A	MET1

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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	GLU86

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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	GLU86	enhance reactivity, modifies pKa, transition state stabiliser
A	TYR164	electrostatic stabiliser

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