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1R3S

Uroporphyrinogen Decarboxylase single mutant D86G in complex with coproporphyrinogen-I

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
A0016831molecular_functioncarboxy-lyase activity
A0042168biological_processheme metabolic process
A0048034biological_processheme O biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues28
DetailsBINDING SITE FOR RESIDUE 1CP A 901
ChainResidue
AARG37
ASER85
AILE87
AMET100
APHE154
ATYR164
APHE217
ASER219
APHE261
AHIS339
AHOH1191
AGLN38
AHOH1291
AHOH1333
AHOH1334
AHOH1362
AHOH1383
AHOH1384
AHOH1387
AHOH1388
AHOH1389
AALA39
AARG41
APHE46
AARG50
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 Residues7
DetailsBINDING:
ChainResidueDetails
AARG37
APHE55
ASER85
AGLY86
ATYR164
ASER219
AHIS339

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Transition state stabilizer
ChainResidueDetails
AGLY86

site_idSWS_FT_FI3
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

222036

PDB entries from 2024-07-03

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