1UU1
Complex of Histidinol-phosphate aminotransferase (HisC) from Thermotoga maritima (Apo-form)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000105 | biological_process | 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 | 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 | 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 | 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 | 14 |
Details | BINDING SITE FOR RESIDUE PMP A1335 |
Chain | Residue |
A | GLY84 |
A | SER201 |
A | LYS202 |
A | ARG210 |
A | HSA1336 |
B | TYR53 |
A | ALA85 |
A | ASP86 |
A | TYR106 |
A | ASN149 |
A | ASP173 |
A | ALA175 |
A | TYR176 |
A | THR199 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE HSA A1336 |
Chain | Residue |
A | ASP86 |
A | TYR106 |
A | SER107 |
A | ASN149 |
A | PHE310 |
A | ARG315 |
A | PMP1335 |
A | HOH2101 |
A | HOH2102 |
B | TYR53 |
B | PHE231 |
site_id | AC3 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PMP B1335 |
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 |
B | HSA1336 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE HSA B1336 |
Chain | Residue |
A | TYR53 |
A | PHE231 |
B | ASP86 |
B | TYR106 |
B | SER107 |
B | CYS108 |
B | ARG315 |
B | PMP1335 |
B | HOH2081 |
B | HOH2082 |
site_id | AC5 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE PMP C1335 |
Chain | Residue |
C | GLY84 |
C | ALA85 |
C | ASP86 |
C | ILE89 |
C | TYR106 |
C | ASN149 |
C | ASP173 |
C | ALA175 |
C | TYR176 |
C | THR199 |
C | SER201 |
C | LYS202 |
C | ARG210 |
C | HSA1336 |
D | TYR53 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE HSA C1336 |
Chain | Residue |
C | ASP86 |
C | TYR106 |
C | SER107 |
C | ASN149 |
C | ARG308 |
C | ARG315 |
C | PMP1335 |
C | HOH2054 |
D | TYR53 |
D | PHE231 |
site_id | AC7 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PMP D1335 |
Chain | Residue |
C | TYR53 |
D | GLY84 |
D | ALA85 |
D | ASP86 |
D | TYR106 |
D | ASN149 |
D | ASP173 |
D | ALA175 |
D | TYR176 |
D | THR199 |
D | SER201 |
D | LYS202 |
D | ARG210 |
D | HSA1336 |
site_id | AC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE HSA D1336 |
Chain | Residue |
C | TYR53 |
C | PHE231 |
D | ASP86 |
D | TYR106 |
D | SER107 |
D | LYS202 |
D | ARG308 |
D | ARG315 |
D | PMP1335 |
D | HOH2088 |
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 |