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2C5Q

Crystal structure of yeast YER010Cp

Functional Information from GO Data
ChainGOidnamespacecontents
A0005575cellular_componentcellular_component
A0008948molecular_functionoxaloacetate decarboxylase activity
A0016829molecular_functionlyase activity
A0019619biological_process3,4-dihydroxybenzoate catabolic process
A0046872molecular_functionmetal ion binding
A0047443molecular_function4-hydroxy-4-methyl-2-oxoglutarate aldolase activity
B0005575cellular_componentcellular_component
B0008948molecular_functionoxaloacetate decarboxylase activity
B0016829molecular_functionlyase activity
B0019619biological_process3,4-dihydroxybenzoate catabolic process
B0046872molecular_functionmetal ion binding
B0047443molecular_function4-hydroxy-4-methyl-2-oxoglutarate aldolase activity
C0005575cellular_componentcellular_component
C0008948molecular_functionoxaloacetate decarboxylase activity
C0016829molecular_functionlyase activity
C0019619biological_process3,4-dihydroxybenzoate catabolic process
C0046872molecular_functionmetal ion binding
C0047443molecular_function4-hydroxy-4-methyl-2-oxoglutarate aldolase activity
D0005575cellular_componentcellular_component
D0008948molecular_functionoxaloacetate decarboxylase activity
D0016829molecular_functionlyase activity
D0019619biological_process3,4-dihydroxybenzoate catabolic process
D0046872molecular_functionmetal ion binding
D0047443molecular_function4-hydroxy-4-methyl-2-oxoglutarate aldolase activity
E0005575cellular_componentcellular_component
E0008948molecular_functionoxaloacetate decarboxylase activity
E0016829molecular_functionlyase activity
E0019619biological_process3,4-dihydroxybenzoate catabolic process
E0046872molecular_functionmetal ion binding
E0047443molecular_function4-hydroxy-4-methyl-2-oxoglutarate aldolase activity
F0005575cellular_componentcellular_component
F0008948molecular_functionoxaloacetate decarboxylase activity
F0016829molecular_functionlyase activity
F0019619biological_process3,4-dihydroxybenzoate catabolic process
F0046872molecular_functionmetal ion binding
F0047443molecular_function4-hydroxy-4-methyl-2-oxoglutarate aldolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A1234
ChainResidue
AILE25
ATHR27
AGLN167
AARG184
AHOH2297
AHOH2298

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B1233
ChainResidue
BALA36
BASN179
BHOH2045
AVAL139
BLEU34
BTHR35

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B1234
ChainResidue
BASP123
BVAL124
BASP125
BGLU126
BHOH2145
CASN180
CHOH2022

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO C1234
ChainResidue
CGLU211
CHOH2291
EVAL64
EASN65
FLYS220
FEDO1235

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO D1234
ChainResidue
DTYR99
DGLY100
DMET103
DARG122
DPRO144

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO D1235
ChainResidue
DILE25
DTHR27
DGLN167
DARG184
DHOH2304
DHOH2305

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO D1236
ChainResidue
DASN65
DILE67
DHOH2306
DHOH2307
DHOH2308
ELYS220
EGLN223

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO D1237
ChainResidue
DLEU34
DTHR35
DALA36
DASP178
DASN179
DGLY181
DHOH2076
FVAL139

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO F1232
ChainResidue
DASN180
FASP123
FVAL124
FASP125
FGLU126
FHOH2158
FHOH2270

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO F1233
ChainResidue
EVAL139
FLEU34
FTHR35
FALA36
FASP178
FASN179
FGLY181
FHOH2050
FHOH2218

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO F1234
ChainResidue
AHOH2274
FARG61
FVAL151
FHOH2271
FHOH2272

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO F1235
ChainResidue
CEDO1234
CHOH2291
FLYS220
FGLN223
FASN224
FHOH2258
FHOH2273

site_idBC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO F1236
ChainResidue
FMET98
FTYR99
FGLY100
FMET103
FARG122
FPRO144
FHOH2274

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY100
DGLY100
DARG122
DASP123
EGLY100
EARG122
EASP123
FGLY100
FARG122
FASP123
AARG122
AASP123
BGLY100
BARG122
BASP123
CGLY100
CARG122
CASP123

site_idSWS_FT_FI2
Number of Residues6
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:22814378
ChainResidueDetails
ASER2
BSER2
CSER2
DSER2
ESER2
FSER2

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PDB entries from 2024-11-06

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