2F8J
Crystal structure of Histidinol-phosphate aminotransferase (EC 2.6.1.9) (Imidazole acetol-phosphate transferase) (tm1040) from Thermotoga maritima at 2.40 A resolution
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 | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0000105 | biological_process | L-histidine biosynthetic process |
| B | 0004400 | molecular_function | histidinol-phosphate transaminase activity |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| C | 0000105 | biological_process | L-histidine biosynthetic process |
| C | 0004400 | molecular_function | histidinol-phosphate transaminase activity |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0042803 | molecular_function | protein homodimerization activity |
| D | 0000105 | biological_process | L-histidine biosynthetic process |
| D | 0004400 | molecular_function | histidinol-phosphate transaminase activity |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PMP A 500 |
| Chain | Residue |
| A | GLY84 |
| A | LYS202 |
| A | ARG210 |
| A | HOH567 |
| B | TYR53 |
| A | ALA85 |
| A | ASP86 |
| A | TYR106 |
| A | ASN149 |
| A | ASP173 |
| A | TYR176 |
| A | THR199 |
| A | SER201 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PMP B 500 |
| Chain | Residue |
| A | TYR53 |
| B | GLY84 |
| B | ALA85 |
| B | ASP86 |
| B | TYR106 |
| B | ASN149 |
| B | ASP173 |
| B | ALA175 |
| B | TYR176 |
| B | THR199 |
| B | SER201 |
| B | LYS202 |
| B | ARG210 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PMP C 500 |
| Chain | Residue |
| C | GLY84 |
| C | ALA85 |
| C | ASP86 |
| C | TYR106 |
| C | ASN149 |
| C | ASP173 |
| C | ALA175 |
| C | TYR176 |
| C | THR199 |
| C | SER201 |
| C | LYS202 |
| C | ARG210 |
| D | TYR53 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PMP D 500 |
| Chain | Residue |
| C | TYR53 |
| D | LEU26 |
| D | GLY84 |
| D | ALA85 |
| D | ASP86 |
| D | TYR106 |
| D | ASN149 |
| D | ASP173 |
| D | ALA175 |
| D | TYR176 |
| D | THR199 |
| D | SER201 |
| D | LYS202 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 501 |
| Chain | Residue |
| A | GLU218 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO C 501 |
| Chain | Residue |
| C | GLU294 |
| C | LEU297 |
| C | GLU298 |
| C | ARG301 |
| C | HOH597 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO C 502 |
| Chain | Residue |
| A | THR302 |
| C | ARG43 |
| C | ARG44 |
| C | LEU45 |
| C | HOH584 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO D 501 |
| Chain | Residue |
| C | GLU87 |
| C | TYR90 |
| C | LEU229 |
| D | GLU87 |
| D | TYR90 |
| D | VAL91 |
| D | LEU229 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 501 |
| Chain | Residue |
| B | LYS76 |
| B | ASN77 |
| B | VAL79 |
| B | SER80 |
| B | ILE221 |
| B | ASN225 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 502 |
| Chain | Residue |
| B | ARG130 |
| B | ILE131 |
| B | GLU133 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 503 |
| Chain | Residue |
| A | ARG51 |
| B | TYR23 |
| B | GLU323 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 504 |
| Chain | Residue |
| B | LYS64 |
| B | SER67 |
| B | TYR68 |
| B | LEU245 |
| B | ASP246 |
| B | ARG248 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO C 503 |
| Chain | Residue |
| C | TYR68 |
| C | PHE251 |
| C | THR255 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 502 |
| Chain | Residue |
| D | TYR68 |
| D | ALA175 |
| D | TYR177 |
| D | GLU178 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 505 |
| Chain | Residue |
| B | GLU252 |
| B | THR255 |
| B | HOH564 |
| B | TYR68 |
| B | GLU178 |
| B | PHE204 |
| B | PHE251 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 502 |
| Chain | Residue |
| A | ARG275 |
| A | GLU289 |
| A | HOH593 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 503 |
| Chain | Residue |
| A | ARG262 |
| A | GLU263 |
| A | ARG280 |
Functional Information from PROSITE/UniProt
| site_id | PS00599 |
| Number of Residues | 10 |
| Details | AA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TFSKAFSLAA |
| Chain | Residue | Details |
| A | THR199-ALA208 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"15007066","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1H1C","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TYR106 | |
| A | ASP173 | |
| A | LYS202 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TYR106 | |
| A | ASP173 | |
| B | PRO57 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| C | PRO57 | |
| D | TYR106 | |
| D | ASP173 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| D | PRO57 | |
| C | TYR106 | |
| C | ASP173 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | TYR106 | |
| B | ASP173 | |
| B | LYS202 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| C | TYR106 | |
| C | ASP173 | |
| C | LYS202 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| D | TYR106 | |
| D | ASP173 | |
| D | LYS202 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | PHE102 | |
| A | ASP173 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | PHE102 | |
| B | ASP173 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| C | PHE102 | |
| C | ASP173 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| D | PHE102 | |
| D | ASP173 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | PRO57 | |
| B | TYR106 | |
| B | ASP173 |
