4R2N
Crystal structure of Rv3772 in complex with its substrate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000105 | biological_process | L-histidine biosynthetic process |
| A | 0004400 | molecular_function | histidinol-phosphate transaminase activity |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0000105 | biological_process | L-histidine biosynthetic process |
| B | 0004400 | molecular_function | histidinol-phosphate transaminase activity |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0000105 | biological_process | L-histidine biosynthetic process |
| C | 0004400 | molecular_function | histidinol-phosphate transaminase activity |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0000105 | biological_process | L-histidine biosynthetic process |
| D | 0004400 | molecular_function | histidinol-phosphate transaminase activity |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP A 401 |
| Chain | Residue |
| A | GLY84 |
| A | THR214 |
| A | SER216 |
| A | LYS217 |
| A | ARG225 |
| A | PHE402 |
| C | TYR54 |
| A | SER85 |
| A | VAL86 |
| A | PHE110 |
| A | CYS153 |
| A | ASN157 |
| A | ASP184 |
| A | ALA186 |
| A | TYR187 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PHE A 402 |
| Chain | Residue |
| A | TYR15 |
| A | VAL86 |
| A | GLU111 |
| A | LEU112 |
| A | ASN157 |
| A | TYR187 |
| A | LYS217 |
| A | ARG330 |
| A | PLP401 |
| C | TYR54 |
| C | PHE246 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EPE A 403 |
| Chain | Residue |
| A | ILE191 |
| A | ARG192 |
| A | ASP193 |
| A | GLY194 |
| A | MET195 |
| A | ARG196 |
| A | LEU267 |
| A | THR270 |
| A | HOH601 |
| A | HOH676 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP B 401 |
| Chain | Residue |
| B | GLY84 |
| B | SER85 |
| B | VAL86 |
| B | PHE110 |
| B | CYS153 |
| B | ASN157 |
| B | ASP184 |
| B | ALA186 |
| B | TYR187 |
| B | THR214 |
| B | SER216 |
| B | LYS217 |
| B | ARG225 |
| B | PHE402 |
| D | TYR54 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PHE B 402 |
| Chain | Residue |
| B | TYR15 |
| B | PHE110 |
| B | GLU111 |
| B | LEU112 |
| B | ASN157 |
| B | TYR187 |
| B | LYS217 |
| B | ARG330 |
| B | PLP401 |
| D | TYR54 |
| D | PHE246 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE EPE B 403 |
| Chain | Residue |
| B | ILE191 |
| B | ARG192 |
| B | ASP193 |
| B | GLY194 |
| B | MET195 |
| B | ARG196 |
| B | LEU267 |
| B | THR270 |
| B | HOH522 |
| B | HOH649 |
| B | HOH691 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP C 401 |
| Chain | Residue |
| A | TYR54 |
| C | GLY84 |
| C | SER85 |
| C | VAL86 |
| C | PHE110 |
| C | CYS153 |
| C | ASN157 |
| C | ASP184 |
| C | ALA186 |
| C | TYR187 |
| C | THR214 |
| C | SER216 |
| C | LYS217 |
| C | ARG225 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PHE C 402 |
| Chain | Residue |
| A | PRO245 |
| A | PHE246 |
| C | PHE110 |
| C | GLU111 |
| C | ARG322 |
| C | HOH651 |
| C | HOH707 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EPE C 403 |
| Chain | Residue |
| C | ARG196 |
| C | LEU267 |
| C | THR270 |
| C | HOH543 |
| C | ILE191 |
| C | ARG192 |
| C | ASP193 |
| C | GLY194 |
| C | MET195 |
| site_id | BC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP D 401 |
| Chain | Residue |
| B | TYR54 |
| D | GLY84 |
| D | SER85 |
| D | VAL86 |
| D | PHE110 |
| D | CYS153 |
| D | ASN157 |
| D | ASP184 |
| D | ALA186 |
| D | TYR187 |
| D | THR214 |
| D | SER216 |
| D | LYS217 |
| D | ARG225 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PHE D 402 |
| Chain | Residue |
| B | ASN57 |
| B | PHE246 |
| D | TYR15 |
| D | VAL16 |
| D | GLU111 |
| D | ARG322 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EPE D 403 |
| Chain | Residue |
| D | ILE191 |
| D | ARG192 |
| D | ASP193 |
| D | GLY194 |
| D | MET195 |
| D | ARG196 |
| D | HOH667 |
| D | HOH668 |
Functional Information from PROSITE/UniProt
| site_id | PS00599 |
| Number of Residues | 10 |
| Details | AA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TFSKAYGLAG |
| Chain | Residue | Details |
| A | THR214-GLY223 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_01513 |
| Chain | Residue | Details |
| A | LYS217 | |
| B | LYS217 | |
| C | LYS217 | |
| D | LYS217 |
