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1R3T

Uroporphyrinogen Decarboxylase single mutant D86G in complex with coproporphyrinogen-III

Functional Information from GO Data
ChainGOidnamespacecontents
A0004853molecular_functionuroporphyrinogen decarboxylase activity
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006778biological_processporphyrin-containing compound metabolic process
A0006779biological_processporphyrin-containing compound biosynthetic process
A0006782biological_processprotoporphyrinogen IX biosynthetic process
A0006783biological_processheme biosynthetic process
A0006784biological_processheme A biosynthetic process
A0006785biological_processheme B biosynthetic process
A0006787biological_processporphyrin-containing compound catabolic process
A0016829molecular_functionlyase activity
A0016831molecular_functioncarboxy-lyase activity
A0042168biological_processheme metabolic process
A0048034biological_processheme O biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE CP3 A 867
ChainResidue
AARG37
APHE84
ASER85
AILE87
APHE154
ATYR164
APHE217
ASER219
AHIS339
AHOH1327
AHOH1333
AGLN38
AHOH1334
AHOH1337
AHOH1338
AHOH1358
AHOH1362
AALA39
AGLY40
AARG41
APHE46
APHE55
AILE82
AILE83

Functional Information from PROSITE/UniProt
site_idPS00906
Number of Residues10
DetailsUROD_1 Uroporphyrinogen decarboxylase signature 1. PVWCMRQAGR
ChainResidueDetails
APRO32-ARG41

site_idPS00907
Number of Residues17
DetailsUROD_2 Uroporphyrinogen decarboxylase signature 2. IGFAGaPWTLmtYmv.EG
ChainResidueDetails
AILE152-GLY168

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:14633982, ECO:0007744|PDB:1R3W, ECO:0007744|PDB:1R3Y
ChainResidueDetails
AARG37
AGLY86
AHIS339

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:14633982, ECO:0007744|PDB:1R3T, ECO:0007744|PDB:1R3W, ECO:0007744|PDB:1R3Y
ChainResidueDetails
AALA39
AARG41

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:14633982, ECO:0007744|PDB:1R3Q, ECO:0007744|PDB:1R3S
ChainResidueDetails
AARG50

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:14633982, ECO:0007744|PDB:1R3Y
ChainResidueDetails
ATYR164

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:14633982, ECO:0007744|PDB:1R3T, ECO:0007744|PDB:1R3W
ChainResidueDetails
ASER219

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000269|PubMed:14633982
ChainResidueDetails
AGLY86

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
ChainResidueDetails
AMET1

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1uro
ChainResidueDetails
ATYR164
AGLY86

site_idMCSA1
Number of Residues5
DetailsM-CSA 914
ChainResidueDetails
AARG37proton shuttle (general acid/base)
AARG41electrostatic stabiliser
AARG50proton shuttle (general acid/base)
AGLY86enhance reactivity, modifies pKa, transition state stabiliser
ATYR164electrostatic stabiliser

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PDB entries from 2025-06-18

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