2C5Q
Crystal structure of yeast YER010Cp
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005575 | cellular_component | cellular_component |
A | 0008948 | molecular_function | oxaloacetate decarboxylase activity |
A | 0016829 | molecular_function | lyase activity |
A | 0019619 | biological_process | 3,4-dihydroxybenzoate catabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0047443 | molecular_function | 4-hydroxy-4-methyl-2-oxoglutarate aldolase activity |
B | 0005575 | cellular_component | cellular_component |
B | 0008948 | molecular_function | oxaloacetate decarboxylase activity |
B | 0016829 | molecular_function | lyase activity |
B | 0019619 | biological_process | 3,4-dihydroxybenzoate catabolic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0047443 | molecular_function | 4-hydroxy-4-methyl-2-oxoglutarate aldolase activity |
C | 0005575 | cellular_component | cellular_component |
C | 0008948 | molecular_function | oxaloacetate decarboxylase activity |
C | 0016829 | molecular_function | lyase activity |
C | 0019619 | biological_process | 3,4-dihydroxybenzoate catabolic process |
C | 0046872 | molecular_function | metal ion binding |
C | 0047443 | molecular_function | 4-hydroxy-4-methyl-2-oxoglutarate aldolase activity |
D | 0005575 | cellular_component | cellular_component |
D | 0008948 | molecular_function | oxaloacetate decarboxylase activity |
D | 0016829 | molecular_function | lyase activity |
D | 0019619 | biological_process | 3,4-dihydroxybenzoate catabolic process |
D | 0046872 | molecular_function | metal ion binding |
D | 0047443 | molecular_function | 4-hydroxy-4-methyl-2-oxoglutarate aldolase activity |
E | 0005575 | cellular_component | cellular_component |
E | 0008948 | molecular_function | oxaloacetate decarboxylase activity |
E | 0016829 | molecular_function | lyase activity |
E | 0019619 | biological_process | 3,4-dihydroxybenzoate catabolic process |
E | 0046872 | molecular_function | metal ion binding |
E | 0047443 | molecular_function | 4-hydroxy-4-methyl-2-oxoglutarate aldolase activity |
F | 0005575 | cellular_component | cellular_component |
F | 0008948 | molecular_function | oxaloacetate decarboxylase activity |
F | 0016829 | molecular_function | lyase activity |
F | 0019619 | biological_process | 3,4-dihydroxybenzoate catabolic process |
F | 0046872 | molecular_function | metal ion binding |
F | 0047443 | molecular_function | 4-hydroxy-4-methyl-2-oxoglutarate aldolase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A1234 |
Chain | Residue |
A | ILE25 |
A | THR27 |
A | GLN167 |
A | ARG184 |
A | HOH2297 |
A | HOH2298 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B1233 |
Chain | Residue |
B | ALA36 |
B | ASN179 |
B | HOH2045 |
A | VAL139 |
B | LEU34 |
B | THR35 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B1234 |
Chain | Residue |
B | ASP123 |
B | VAL124 |
B | ASP125 |
B | GLU126 |
B | HOH2145 |
C | ASN180 |
C | HOH2022 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO C1234 |
Chain | Residue |
C | GLU211 |
C | HOH2291 |
E | VAL64 |
E | ASN65 |
F | LYS220 |
F | EDO1235 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO D1234 |
Chain | Residue |
D | TYR99 |
D | GLY100 |
D | MET103 |
D | ARG122 |
D | PRO144 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO D1235 |
Chain | Residue |
D | ILE25 |
D | THR27 |
D | GLN167 |
D | ARG184 |
D | HOH2304 |
D | HOH2305 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO D1236 |
Chain | Residue |
D | ASN65 |
D | ILE67 |
D | HOH2306 |
D | HOH2307 |
D | HOH2308 |
E | LYS220 |
E | GLN223 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO D1237 |
Chain | Residue |
D | LEU34 |
D | THR35 |
D | ALA36 |
D | ASP178 |
D | ASN179 |
D | GLY181 |
D | HOH2076 |
F | VAL139 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO F1232 |
Chain | Residue |
D | ASN180 |
F | ASP123 |
F | VAL124 |
F | ASP125 |
F | GLU126 |
F | HOH2158 |
F | HOH2270 |
site_id | BC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO F1233 |
Chain | Residue |
E | VAL139 |
F | LEU34 |
F | THR35 |
F | ALA36 |
F | ASP178 |
F | ASN179 |
F | GLY181 |
F | HOH2050 |
F | HOH2218 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO F1234 |
Chain | Residue |
A | HOH2274 |
F | ARG61 |
F | VAL151 |
F | HOH2271 |
F | HOH2272 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO F1235 |
Chain | Residue |
C | EDO1234 |
C | HOH2291 |
F | LYS220 |
F | GLN223 |
F | ASN224 |
F | HOH2258 |
F | HOH2273 |
site_id | BC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO F1236 |
Chain | Residue |
F | MET98 |
F | TYR99 |
F | GLY100 |
F | MET103 |
F | ARG122 |
F | PRO144 |
F | HOH2274 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | GLY100 | |
D | GLY100 | |
D | ARG122 | |
D | ASP123 | |
E | GLY100 | |
E | ARG122 | |
E | ASP123 | |
F | GLY100 | |
F | ARG122 | |
F | ASP123 | |
A | ARG122 | |
A | ASP123 | |
B | GLY100 | |
B | ARG122 | |
B | ASP123 | |
C | GLY100 | |
C | ARG122 | |
C | ASP123 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | MOD_RES: N-acetylserine => ECO:0007744|PubMed:22814378 |
Chain | Residue | Details |
A | SER2 | |
B | SER2 | |
C | SER2 | |
D | SER2 | |
E | SER2 | |
F | SER2 |