1SFF
Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate
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 | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 1301 |
Chain | Residue |
A | LYS151 |
A | ASN153 |
A | TYR394 |
A | HOH1462 |
C | LYS192 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 1302 |
Chain | Residue |
B | LYS151 |
B | ASN153 |
B | TYR394 |
D | HOH1512 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 C 1303 |
Chain | Residue |
A | LYS192 |
A | HOH1471 |
C | LYS151 |
C | ASN153 |
C | TYR394 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 D 1304 |
Chain | Residue |
B | LYS192 |
D | LYS151 |
D | ASN153 |
D | TYR394 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 1305 |
Chain | Residue |
B | LYS5 |
B | ARG381 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 D 1306 |
Chain | Residue |
D | LYS5 |
D | ARG381 |
D | HOH1587 |
D | HOH1680 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1307 |
Chain | Residue |
A | ILE184 |
A | ARG224 |
A | HOH1500 |
A | HOH1619 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 1308 |
Chain | Residue |
B | ARG224 |
B | HOH1517 |
B | HOH1643 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 C 1309 |
Chain | Residue |
C | ARG224 |
C | HOH1521 |
C | HOH1570 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 D 1310 |
Chain | Residue |
D | HIS188 |
D | ARG224 |
D | HOH1564 |
D | HOH1577 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 C 1311 |
Chain | Residue |
A | GLN419 |
A | HOH1661 |
A | HOH1665 |
C | LYS71 |
C | HOH1547 |
D | ARG29 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A 1401 |
Chain | Residue |
A | ASP45 |
A | ALA47 |
A | GLY48 |
A | GLY49 |
A | HIS57 |
B | THR76 |
B | VAL80 |
B | LEU81 |
site_id | BC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO B 1402 |
Chain | Residue |
A | THR76 |
A | VAL80 |
A | LEU81 |
B | ASP45 |
B | ALA47 |
B | GLY48 |
B | GLY49 |
B | HIS57 |
site_id | BC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO C 1403 |
Chain | Residue |
C | ASP45 |
C | ALA47 |
C | GLY48 |
C | GLY49 |
C | HIS57 |
D | THR76 |
D | VAL80 |
D | LEU81 |
site_id | BC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO D 1404 |
Chain | Residue |
C | THR76 |
C | VAL80 |
C | LEU81 |
D | ASP45 |
D | ALA47 |
D | GLY48 |
D | GLY49 |
D | HIS57 |
site_id | BC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO B 1405 |
Chain | Residue |
B | GLY164 |
B | HIS165 |
B | TYR167 |
B | HOH1550 |
B | HOH1585 |
D | GLY164 |
D | HIS165 |
D | TYR167 |
site_id | BC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 1406 |
Chain | Residue |
A | GLN69 |
A | LYS72 |
A | LEU73 |
A | PRO85 |
A | HOH1518 |
B | ALA27 |
B | ASP28 |
site_id | BC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO C 1407 |
Chain | Residue |
C | GLN69 |
C | LYS72 |
C | LEU73 |
C | PRO85 |
C | HOH1598 |
D | ALA27 |
D | ASP28 |
D | HOH1543 |
site_id | CC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO D 1408 |
Chain | Residue |
C | ALA27 |
C | ASP28 |
D | GLN69 |
D | LYS72 |
D | LEU73 |
D | PRO85 |
D | HOH1555 |
site_id | CC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO C 1409 |
Chain | Residue |
A | MET162 |
A | PRO163 |
A | EDO1410 |
A | HOH1452 |
A | HOH1568 |
C | TYR167 |
C | ASP194 |
site_id | CC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO A 1410 |
Chain | Residue |
A | GLY164 |
A | HIS165 |
A | TYR167 |
A | HOH1532 |
A | HOH1568 |
C | GLY164 |
C | HIS165 |
C | TYR167 |
C | EDO1409 |
site_id | CC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 1411 |
Chain | Residue |
A | GLN9 |
D | GLN95 |
D | LYS96 |
D | PRO98 |
D | GLU255 |
site_id | CC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO D 1412 |
Chain | Residue |
D | ILE22 |
D | HIS23 |
D | PRO24 |
D | ARG381 |
site_id | CC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO D 1413 |
Chain | Residue |
C | PRO275 |
C | ASN301 |
C | ILE303 |
D | PRO275 |
D | ASN301 |
D | ILE303 |
site_id | CC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 1414 |
Chain | Residue |
B | ILE22 |
B | HIS23 |
B | PRO24 |
B | ARG381 |
site_id | CC8 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE IK2 A 450 |
Chain | Residue |
A | GLY111 |
A | SER112 |
A | TYR138 |
A | HIS139 |
A | ARG141 |
A | GLU206 |
A | ASP239 |
A | VAL241 |
A | GLN242 |
A | LYS268 |
A | HOH1414 |
A | HOH1416 |
A | HOH1459 |
A | HOH1523 |
A | HOH1624 |
A | HOH1650 |
A | HOH1740 |
B | GLN79 |
B | GLY296 |
B | THR297 |
B | HOH1450 |
site_id | CC9 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE IK2 B 450 |
Chain | Residue |
A | GLN79 |
A | GLY296 |
A | THR297 |
B | THR110 |
B | GLY111 |
B | SER112 |
B | TYR138 |
B | HIS139 |
B | ARG141 |
B | GLU206 |
B | ASP239 |
B | VAL241 |
B | GLN242 |
B | LYS268 |
B | HOH1427 |
B | HOH1431 |
B | HOH1432 |
B | HOH1436 |
B | HOH1440 |
B | HOH1580 |
B | HOH1635 |
site_id | DC1 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE IK2 C 450 |
Chain | Residue |
C | THR110 |
C | GLY111 |
C | SER112 |
C | TYR138 |
C | HIS139 |
C | ARG141 |
C | GLU206 |
C | ASP239 |
C | VAL241 |
C | GLN242 |
C | LYS268 |
C | HOH1410 |
C | HOH1424 |
C | HOH1445 |
C | HOH1463 |
C | HOH1516 |
C | HOH1615 |
D | GLN79 |
D | THR297 |
D | HOH1442 |
site_id | DC2 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE IK2 D 450 |
Chain | Residue |
C | GLN79 |
C | GLY296 |
C | THR297 |
C | HOH1428 |
D | GLY111 |
D | SER112 |
D | TYR138 |
D | HIS139 |
D | ARG141 |
D | GLU206 |
D | ASP239 |
D | VAL241 |
D | GLN242 |
D | LYS268 |
D | HOH1416 |
D | HOH1429 |
D | HOH1435 |
D | HOH1505 |
D | HOH1559 |
D | HOH1599 |
D | HOH1718 |
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 |