4E3Q
PMP-bound form of Aminotransferase crystal structure from Vibrio fluvialis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003867 | molecular_function | 4-aminobutyrate transaminase activity |
| A | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009102 | biological_process | biotin biosynthetic process |
| A | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0003867 | molecular_function | 4-aminobutyrate transaminase activity |
| B | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009102 | biological_process | biotin biosynthetic process |
| B | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0003867 | molecular_function | 4-aminobutyrate transaminase activity |
| C | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009102 | biological_process | biotin biosynthetic process |
| C | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0003867 | molecular_function | 4-aminobutyrate transaminase activity |
| D | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0009102 | biological_process | biotin biosynthetic process |
| D | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 501 |
| Chain | Residue |
| A | VAL101 |
| A | GLU102 |
| A | SER104 |
| A | PHE106 |
| A | HOH693 |
| A | HOH765 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 502 |
| Chain | Residue |
| B | GLN5 |
| B | SER6 |
| B | ALA9 |
| A | GLN5 |
| A | SER6 |
| A | ALA9 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BEN A 503 |
| Chain | Residue |
| A | ARG48 |
| A | TYR49 |
| A | ASP409 |
| A | LEU410 |
| A | GLY411 |
| D | LYS335 |
| D | ASP338 |
| D | ASN342 |
| D | GLU343 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BEN A 504 |
| Chain | Residue |
| A | LYS335 |
| A | ASP338 |
| A | ASN342 |
| A | GLU343 |
| D | ARG48 |
| D | ASP409 |
| D | GLY411 |
| D | HOH816 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PMP A 505 |
| Chain | Residue |
| A | SER116 |
| A | GLY117 |
| A | SER118 |
| A | TYR150 |
| A | HIS151 |
| A | GLU223 |
| A | ASP256 |
| A | VAL258 |
| A | ILE259 |
| A | LYS285 |
| A | HOH604 |
| A | HOH606 |
| A | HOH609 |
| A | HOH630 |
| B | PHE321 |
| B | THR322 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 501 |
| Chain | Residue |
| B | VAL101 |
| B | GLU102 |
| B | SER104 |
| B | PHE106 |
| B | HOH796 |
| B | HOH890 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE BEN B 502 |
| Chain | Residue |
| B | ARG48 |
| B | LYS335 |
| B | ASP338 |
| B | ASN342 |
| B | GLU343 |
| B | ASP409 |
| B | GLY411 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PMP B 503 |
| Chain | Residue |
| A | PHE321 |
| A | THR322 |
| B | SER116 |
| B | GLY117 |
| B | SER118 |
| B | TYR150 |
| B | HIS151 |
| B | GLU223 |
| B | ASP256 |
| B | VAL258 |
| B | ILE259 |
| B | LYS285 |
| B | HOH602 |
| B | HOH611 |
| B | HOH615 |
| B | HOH654 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA C 501 |
| Chain | Residue |
| C | VAL101 |
| C | GLU102 |
| C | SER104 |
| C | PHE106 |
| C | HOH799 |
| C | HOH826 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 C 502 |
| Chain | Residue |
| C | PRO4 |
| C | GLN5 |
| C | SER6 |
| C | ALA9 |
| D | GLN5 |
| D | SER6 |
| D | ALA9 |
| site_id | BC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PMP C 503 |
| Chain | Residue |
| C | HOH631 |
| C | HOH635 |
| C | HOH705 |
| D | PHE321 |
| D | THR322 |
| C | SER116 |
| C | GLY117 |
| C | SER118 |
| C | TYR150 |
| C | HIS151 |
| C | GLU223 |
| C | ASP256 |
| C | VAL258 |
| C | ILE259 |
| C | LYS285 |
| C | HOH605 |
| C | HOH619 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA D 501 |
| Chain | Residue |
| D | VAL101 |
| D | GLU102 |
| D | SER104 |
| D | PHE106 |
| D | HOH687 |
| D | HOH767 |
| site_id | BC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PMP D 502 |
| Chain | Residue |
| C | PHE321 |
| C | THR322 |
| D | SER116 |
| D | GLY117 |
| D | SER118 |
| D | TYR150 |
| D | HIS151 |
| D | GLU223 |
| D | ASP256 |
| D | VAL258 |
| D | ILE259 |
| D | LYS285 |
| D | HOH610 |
| D | HOH615 |
| D | HOH639 |
| D | HOH649 |
| D | HOH800 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 38 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. VIsDEVic.GFgRtGntwgcvtydftp....DAIisSKnltAG |
| Chain | Residue | Details |
| A | VAL253-GLY290 |
