1SF2
Structure of E. coli gamma-aminobutyrate aminotransferase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003867 | molecular_function | 4-aminobutyrate transaminase activity |
| A | 0003992 | molecular_function | N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
| A | 0009450 | biological_process | gamma-aminobutyric acid catabolic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0034386 | molecular_function | 4-aminobutyrate:2-oxoglutarate transaminase activity |
| A | 0042450 | biological_process | arginine biosynthetic process via ornithine |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0047589 | molecular_function | 5-aminovalerate transaminase activity |
| B | 0003867 | molecular_function | 4-aminobutyrate transaminase activity |
| B | 0003992 | molecular_function | N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
| B | 0009450 | biological_process | gamma-aminobutyric acid catabolic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0034386 | molecular_function | 4-aminobutyrate:2-oxoglutarate transaminase activity |
| B | 0042450 | biological_process | arginine biosynthetic process via ornithine |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0047589 | molecular_function | 5-aminovalerate transaminase activity |
| C | 0003867 | molecular_function | 4-aminobutyrate transaminase activity |
| C | 0003992 | molecular_function | N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
| C | 0009450 | biological_process | gamma-aminobutyric acid catabolic process |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0034386 | molecular_function | 4-aminobutyrate:2-oxoglutarate transaminase activity |
| C | 0042450 | biological_process | arginine biosynthetic process via ornithine |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0047589 | molecular_function | 5-aminovalerate transaminase activity |
| D | 0003867 | molecular_function | 4-aminobutyrate transaminase activity |
| D | 0003992 | molecular_function | N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
| D | 0009450 | biological_process | gamma-aminobutyric acid catabolic process |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0034386 | molecular_function | 4-aminobutyrate:2-oxoglutarate transaminase activity |
| D | 0042450 | biological_process | arginine biosynthetic process via ornithine |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0047589 | molecular_function | 5-aminovalerate transaminase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1101 |
| Chain | Residue |
| A | HIS188 |
| A | ARG224 |
| A | HOH1393 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1102 |
| Chain | Residue |
| B | ARG381 |
| B | HOH1356 |
| B | HOH1381 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1103 |
| Chain | Residue |
| B | ILE184 |
| B | HIS188 |
| B | ARG224 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1104 |
| Chain | Residue |
| C | HIS188 |
| C | ARG224 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1105 |
| Chain | Residue |
| D | ILE184 |
| D | HIS188 |
| D | ARG224 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1106 |
| Chain | Residue |
| B | HOH1376 |
| D | LYS5 |
| D | ARG381 |
| D | HOH1284 |
| D | HOH1465 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1107 |
| Chain | Residue |
| A | LYS151 |
| A | ASN153 |
| A | TYR394 |
| A | HOH1273 |
| C | LYS192 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1108 |
| Chain | Residue |
| B | ASN153 |
| B | TYR394 |
| D | LYS192 |
| D | HOH1474 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1109 |
| Chain | Residue |
| B | LYS192 |
| B | HOH1318 |
| D | ASN153 |
| D | TYR394 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1110 |
| Chain | Residue |
| A | LYS192 |
| C | ASN153 |
| C | TYR394 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1111 |
| Chain | Residue |
| A | GLN419 |
| A | HOH1449 |
| C | LYS71 |
| D | ARG29 |
| D | HOH1342 |
| site_id | BC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP A 450 |
| Chain | Residue |
| A | THR110 |
| A | GLY111 |
| A | SER112 |
| A | TYR138 |
| A | HIS139 |
| A | GLU206 |
| A | ASP239 |
| A | VAL241 |
| A | GLN242 |
| A | LYS268 |
| A | HOH1215 |
| A | HOH1219 |
| A | HOH1224 |
| A | HOH1278 |
| A | HOH1303 |
| A | HOH1334 |
| B | THR297 |
| site_id | BC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP B 450 |
| Chain | Residue |
| A | THR297 |
| A | HOH1263 |
| B | THR110 |
| B | GLY111 |
| B | SER112 |
| B | TYR138 |
| B | HIS139 |
| B | GLU206 |
| B | ASP239 |
| B | VAL241 |
| B | GLN242 |
| B | LYS268 |
| B | HOH1203 |
| B | HOH1210 |
| B | HOH1218 |
| B | HOH1246 |
| site_id | BC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP C 450 |
| Chain | Residue |
| C | GLY111 |
| C | SER112 |
| C | TYR138 |
| C | HIS139 |
| C | GLU206 |
| C | ASP239 |
| C | VAL241 |
| C | GLN242 |
| C | LYS268 |
| C | HOH1225 |
| C | HOH1230 |
| C | HOH1272 |
| D | THR297 |
| D | HOH1257 |
| site_id | BC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP D 450 |
| Chain | Residue |
| D | HOH1222 |
| D | HOH1225 |
| D | HOH1236 |
| D | HOH1243 |
| D | HOH1471 |
| C | THR297 |
| D | THR110 |
| D | GLY111 |
| D | SER112 |
| D | TYR138 |
| D | HIS139 |
| D | GLU206 |
| D | ASP239 |
| D | VAL241 |
| D | GLN242 |
| D | LYS268 |
| D | HOH1213 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 1201 |
| Chain | Residue |
| A | THR76 |
| A | LEU81 |
| B | ASP45 |
| B | ALA47 |
| B | GLY48 |
| B | GLY49 |
| B | HIS57 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 1202 |
| Chain | Residue |
| B | HIS23 |
| B | PRO24 |
| B | ARG381 |
| B | HOH1327 |
| site_id | BC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO C 1203 |
| Chain | Residue |
| A | GLY164 |
| A | HIS165 |
| A | VAL166 |
| A | TYR167 |
| C | GLY164 |
| C | HIS165 |
| C | TYR167 |
| site_id | CC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EDO D 1204 |
| Chain | Residue |
| B | GLY164 |
| B | HIS165 |
| B | VAL166 |
| B | TYR167 |
| D | GLY164 |
| D | HIS165 |
| D | VAL166 |
| D | TYR167 |
| D | HOH1227 |
| D | HOH1402 |
| site_id | CC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO D 1205 |
| Chain | Residue |
| C | THR76 |
| C | VAL80 |
| D | ASP45 |
| D | ALA47 |
| D | GLY48 |
| D | GLY49 |
| D | HIS57 |
| site_id | CC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C 1206 |
| Chain | Residue |
| C | PRO275 |
| C | ASN301 |
| D | PRO275 |
| D | ASN301 |
| site_id | CC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 1207 |
| Chain | Residue |
| D | HIS23 |
| D | PRO24 |
| D | ARG381 |
| D | HOH1410 |
| site_id | CC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 1208 |
| Chain | Residue |
| A | ASP45 |
| A | ALA47 |
| A | GLY48 |
| A | GLY49 |
| A | HIS57 |
| B | THR76 |
| B | VAL80 |
| B | LEU81 |
| site_id | CC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO C 1209 |
| Chain | Residue |
| C | ASP45 |
| C | ALA47 |
| C | GLY48 |
| C | GLY49 |
| C | HIS57 |
| D | THR76 |
| D | VAL80 |
| D | LEU81 |
| site_id | CC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 1210 |
| Chain | Residue |
| A | GLN69 |
| A | LEU73 |
| A | PRO85 |
| B | ASP28 |
| site_id | CC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO C 1211 |
| Chain | Residue |
| C | GLN69 |
| C | LEU73 |
| C | PRO85 |
| D | ALA27 |
| D | ASP28 |
| site_id | CC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO D 1212 |
| Chain | Residue |
| B | TYR167 |
| D | TYR167 |
| D | ARG168 |
| D | ILE190 |
| D | HOH1318 |
| D | HOH1346 |
| D | HOH1385 |
| site_id | DC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 1213 |
| Chain | Residue |
| A | LYS5 |
| A | GLN9 |
| D | LYS96 |
| D | PRO98 |
| D | GLU255 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 38 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIaDEVqsgAG.RtGtlfameqmgvap....DLTtfAKsiaGG |
| Chain | Residue | Details |
| A | LEU236-GLY273 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15323550, ECO:0000269|PubMed:15723541 |
| Chain | Residue | Details |
| C | THR297 | |
| D | GLY111 | |
| D | GLN242 | |
| D | THR297 | |
| A | GLY111 | |
| A | GLN242 | |
| A | THR297 | |
| B | GLY111 | |
| B | GLN242 | |
| B | THR297 | |
| C | GLY111 | |
| C | GLN242 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:15323550, ECO:0000269|PubMed:15723541, ECO:0007744|PDB:1SF2, ECO:0007744|PDB:1SZS, ECO:0007744|PDB:1SZU |
| Chain | Residue | Details |
| A | LYS268 | |
| B | LYS268 | |
| C | LYS268 | |
| D | LYS268 |
