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 | 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 | 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 | 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 | 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 | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:15007066, ECO:0007744|PDB:1H1C |
Chain | Residue | Details |
A | LYS202 | |
B | LYS202 | |
C | LYS202 | |
D | LYS202 |
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 |