1SZU
The structure of gamma-aminobutyrate aminotransferase mutant: V241A
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 1001 |
| Chain | Residue |
| A | ARG224 |
| A | HOH1725 |
| A | HOH1808 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1002 |
| Chain | Residue |
| B | LYS5 |
| B | ARG381 |
| B | HOH1710 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1003 |
| Chain | Residue |
| B | ILE184 |
| B | HIS188 |
| B | ARG224 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1004 |
| Chain | Residue |
| C | HIS188 |
| C | ARG224 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1005 |
| Chain | Residue |
| D | ILE184 |
| D | ARG224 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1006 |
| Chain | Residue |
| B | HOH1725 |
| D | LYS5 |
| D | ARG381 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1007 |
| Chain | Residue |
| A | LYS151 |
| A | ASN153 |
| A | TYR394 |
| C | LYS192 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1008 |
| Chain | Residue |
| B | ASN153 |
| B | TYR394 |
| D | LYS192 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1009 |
| Chain | Residue |
| B | LYS192 |
| D | LYS151 |
| D | TYR394 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1010 |
| Chain | Residue |
| A | LYS192 |
| C | ASN153 |
| C | TYR394 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1011 |
| Chain | Residue |
| A | GLN419 |
| A | HOH1768 |
| C | LYS71 |
| D | ARG29 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 1021 |
| Chain | Residue |
| A | THR76 |
| A | VAL80 |
| A | LEU81 |
| B | ASP45 |
| B | ALA47 |
| B | GLY48 |
| B | GLY49 |
| B | HIS57 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 1022 |
| Chain | Residue |
| B | HIS23 |
| B | ARG381 |
| B | HOH1820 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 1023 |
| Chain | Residue |
| A | GLY164 |
| A | HIS165 |
| A | TYR167 |
| C | GLY164 |
| C | HIS165 |
| C | VAL166 |
| C | TYR167 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 1024 |
| Chain | Residue |
| B | GLY164 |
| B | HIS165 |
| B | VAL166 |
| B | TYR167 |
| B | HOH1579 |
| D | HIS165 |
| D | VAL166 |
| D | TYR167 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO D 1025 |
| Chain | Residue |
| C | THR76 |
| C | VAL80 |
| D | ASP45 |
| D | ALA47 |
| D | GLY48 |
| D | GLY49 |
| D | HIS57 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 1026 |
| Chain | Residue |
| C | PRO275 |
| C | ASN301 |
| D | PRO275 |
| D | ASN301 |
| D | ILE303 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO D 1027 |
| Chain | Residue |
| D | ILE22 |
| D | HIS23 |
| D | ARG381 |
| site_id | CC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 1028 |
| Chain | Residue |
| A | ASP45 |
| A | ALA47 |
| A | GLY48 |
| A | GLY49 |
| A | HIS57 |
| B | THR76 |
| B | VAL80 |
| B | LEU81 |
| site_id | CC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO C 1029 |
| Chain | Residue |
| C | ASP45 |
| C | ALA47 |
| C | GLY48 |
| C | GLY49 |
| C | HIS57 |
| D | THR76 |
| D | VAL80 |
| D | LEU81 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1030 |
| Chain | Residue |
| A | GLN69 |
| A | LYS72 |
| A | LEU73 |
| A | PRO85 |
| B | ASP28 |
| B | HOH1747 |
| site_id | CC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 1031 |
| Chain | Residue |
| C | HOH1658 |
| D | ALA27 |
| D | ASP28 |
| C | GLN69 |
| C | LEU73 |
| C | PRO85 |
| site_id | CC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 1032 |
| Chain | Residue |
| B | TYR167 |
| B | HOH1745 |
| D | TYR167 |
| D | ARG168 |
| D | HOH1695 |
| site_id | CC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 1033 |
| Chain | Residue |
| A | GLN9 |
| D | GLN95 |
| D | LYS96 |
| D | PRO98 |
| D | GLU255 |
| site_id | CC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO C 1034 |
| Chain | Residue |
| C | GLN79 |
| C | GLY292 |
| C | LEU294 |
| C | HOH1775 |
| D | GLY18 |
| D | GLY20 |
| D | ILE22 |
| site_id | CC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP A 1466 |
| Chain | Residue |
| A | GLY111 |
| A | SER112 |
| A | TYR138 |
| A | GLU206 |
| A | ASP239 |
| A | ALA241 |
| A | GLN242 |
| A | LYS268 |
| A | HOH1568 |
| A | HOH1572 |
| A | HOH1577 |
| A | HOH1814 |
| B | GLY296 |
| B | THR297 |
| B | HOH1636 |
| site_id | CC9 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP B 1467 |
| Chain | Residue |
| A | THR297 |
| A | HOH1614 |
| B | THR110 |
| B | GLY111 |
| B | SER112 |
| B | TYR138 |
| B | HIS139 |
| B | GLU206 |
| B | ASP239 |
| B | ALA241 |
| B | GLN242 |
| B | LYS268 |
| B | HOH1574 |
| B | HOH1582 |
| B | HOH1611 |
| B | HOH1814 |
| site_id | DC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP C 1468 |
| Chain | Residue |
| C | THR110 |
| C | GLY111 |
| C | SER112 |
| C | TYR138 |
| C | HIS139 |
| C | GLU206 |
| C | ASP239 |
| C | ALA241 |
| C | GLN242 |
| C | LYS268 |
| C | HOH1582 |
| C | HOH1585 |
| C | HOH1588 |
| C | HOH1627 |
| D | GLY296 |
| D | THR297 |
| D | HOH1613 |
| site_id | DC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP D 1469 |
| Chain | Residue |
| C | THR297 |
| C | HOH1586 |
| D | THR110 |
| D | GLY111 |
| D | SER112 |
| D | TYR138 |
| D | HIS139 |
| D | GLU206 |
| D | ASP239 |
| D | ALA241 |
| D | GLN242 |
| D | LYS268 |
| D | HOH1570 |
| D | HOH1580 |
| D | HOH1583 |
| D | HOH1808 |
| D | HOH1811 |
| site_id | DC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PMP A 1566 |
| Chain | Residue |
| A | THR110 |
| A | GLY111 |
| A | SER112 |
| A | TYR138 |
| A | HIS139 |
| A | GLU206 |
| A | GLU211 |
| A | ASP239 |
| A | ALA241 |
| A | GLN242 |
| A | LYS268 |
| A | HOH1568 |
| A | HOH1572 |
| A | HOH1577 |
| A | HOH1811 |
| A | HOH1814 |
| B | THR297 |
| B | HOH1636 |
| site_id | DC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE PMP B 1567 |
| Chain | Residue |
| A | THR297 |
| A | HOH1614 |
| B | THR110 |
| B | GLY111 |
| B | SER112 |
| B | TYR138 |
| B | HIS139 |
| B | GLU206 |
| B | GLU211 |
| B | ASP239 |
| B | ALA241 |
| B | GLN242 |
| B | LYS268 |
| B | HOH1574 |
| B | HOH1582 |
| B | HOH1611 |
| B | HOH1616 |
| B | HOH1811 |
| B | HOH1814 |
| B | HOH1817 |
| site_id | DC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PMP C 1568 |
| Chain | Residue |
| C | THR110 |
| C | GLY111 |
| C | SER112 |
| C | TYR138 |
| C | HIS139 |
| C | GLU206 |
| C | ASP239 |
| C | ALA241 |
| C | GLN242 |
| C | LYS268 |
| C | HOH1582 |
| C | HOH1585 |
| C | HOH1588 |
| C | HOH1627 |
| C | HOH1774 |
| D | THR297 |
| D | HOH1613 |
| site_id | DC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE PMP D 1569 |
| Chain | Residue |
| C | THR297 |
| C | HOH1586 |
| D | THR110 |
| D | GLY111 |
| D | SER112 |
| D | TYR138 |
| D | HIS139 |
| D | GLU206 |
| D | GLU211 |
| D | ASP239 |
| D | ALA241 |
| D | GLN242 |
| D | LYS268 |
| D | HOH1570 |
| D | HOH1580 |
| D | HOH1583 |
| D | HOH1808 |
| D | HOH1810 |
| D | HOH1811 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 38 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIaDEAqsgAG.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 |
| A | GLY111 | |
| D | GLY111 | |
| D | GLN242 | |
| D | THR297 | |
| A | GLN242 | |
| A | THR297 | |
| B | GLY111 | |
| B | GLN242 | |
| B | THR297 | |
| C | GLY111 | |
| C | GLN242 | |
| C | THR297 |
| 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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TYR138 | |
| A | LYS268 | |
| A | ASP239 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | TYR138 | |
| B | LYS268 | |
| B | ASP239 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| C | TYR138 | |
| C | LYS268 | |
| C | ASP239 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| D | TYR138 | |
| D | LYS268 | |
| D | ASP239 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | LYS268 | |
| A | HIS139 | |
| A | ASP239 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | LYS268 | |
| B | HIS139 | |
| B | ASP239 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| C | LYS268 | |
| C | HIS139 | |
| C | ASP239 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| D | LYS268 | |
| D | HIS139 | |
| D | ASP239 |
