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3BK0

Crystal Structure of Human Orotidine 5'-monophosphate Decarboxylase Complexed with 5-CN-UMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004590molecular_functionorotidine-5'-phosphate decarboxylase activity
A0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
A0044205biological_process'de novo' UMP biosynthetic process
B0004590molecular_functionorotidine-5'-phosphate decarboxylase activity
B0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
B0044205biological_process'de novo' UMP biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 3001
ChainResidue
AGLY39
AGLU43

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE CNU A 1000
ChainResidue
ASER183
AILE212
APRO228
AGLN241
ATYR243
AGLY261
AARG262
AHOH3002
AHOH3006
AHOH3074
BASP128
BTHR132
ASER68
AASP70
ALYS92
AHIS94
AASP123
AILE179
AMET182

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE CNU B 1001
ChainResidue
AASP128
AILE129
ATHR132
BSER68
BASP70
BLYS92
BHIS94
BASP123
BILE179
BMET182
BSER183
BILE212
BPRO228
BGLN241
BTYR243
BGLY261
BARG262
BHOH1002
BHOH1005
BHOH1015

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 2000
ChainResidue
ALYS53
AALA113
AGLU117
APHE118
AASP149
AHOH3099

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 2001
ChainResidue
AARG46
AHIS48
APRO49
ASER205
AHOH3117

Functional Information from PROSITE/UniProt
site_idPS00156
Number of Residues14
DetailsOMPDECASE Orotidine 5'-phosphate decarboxylase active site. IFeDrKfaDIGnTV
ChainResidueDetails
AILE120-VAL133

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: For OMPdecase activity => ECO:0000269|PubMed:18184586
ChainResidueDetails
AASP123
ALYS125
AASP128
BASP123
BLYS125
BASP128

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:18184586, ECO:0007744|PDB:2QCD
ChainResidueDetails
ASER68
AASP128
ATHR132
BSER68
BASP128
BTHR132

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:18184586, ECO:0007744|PDB:2QCD, ECO:0007744|PDB:2QCH
ChainResidueDetails
AASP70
ASER183
AGLN241
AGLY261
BASP70
BSER183
BGLN241
BGLY261

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:18184586, ECO:0007744|PDB:2QCL
ChainResidueDetails
ALYS92
ALYS125
BLYS92
BLYS125

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dbt
ChainResidueDetails
AASP123
ALYS125

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dbt
ChainResidueDetails
BASP123
BLYS125

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1dbt
ChainResidueDetails
ALYS92
AASP123
ALYS125
AASP128

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1dbt
ChainResidueDetails
BLYS92
BASP123
BLYS125
BASP128

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PDB entries from 2024-07-10

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