1O62
Crystal structure of the apo form of a PLP-dependent enzyme
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000271 | biological_process | polysaccharide biosynthetic process |
A | 0008483 | molecular_function | transaminase activity |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0047302 | molecular_function | UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose transaminase activity |
B | 0000271 | biological_process | polysaccharide biosynthetic process |
B | 0008483 | molecular_function | transaminase activity |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0047302 | molecular_function | UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose transaminase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT B 395 |
Chain | Residue |
B | ARG65 |
B | LYS204 |
B | TYR208 |
B | HOH431 |
B | HOH464 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACT A 395 |
Chain | Residue |
A | TYR226 |
B | TYR91 |
B | ACT396 |
B | HOH523 |
A | HIS61 |
A | TYR91 |
A | LEU92 |
A | TYR224 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACT B 396 |
Chain | Residue |
A | TYR91 |
A | ACT395 |
A | HOH550 |
B | HIS61 |
B | TYR91 |
B | LEU92 |
B | TYR224 |
B | TYR226 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE BME A 401 |
Chain | Residue |
A | CYS90 |
A | VAL340 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE BME A 402 |
Chain | Residue |
A | CYS119 |
A | LYS121 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE BME A 403 |
Chain | Residue |
A | CYS361 |
A | LEU362 |
A | HOH510 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE BME B 401 |
Chain | Residue |
B | CYS90 |
B | VAL340 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BME B 402 |
Chain | Residue |
A | LYS306 |
B | CYS297 |
B | GLN298 |
B | LYS299 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BME B 403 |
Chain | Residue |
B | ARG329 |
B | CYS361 |
B | LEU362 |
B | HOH498 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1b9h |
Chain | Residue | Details |
B | ASP155 | |
B | PHE82 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1b9h |
Chain | Residue | Details |
A | ALA28 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1b9h |
Chain | Residue | Details |
A | ASP155 | |
A | LYS184 | |
A | PHE82 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1b9h |
Chain | Residue | Details |
B | ASP155 | |
B | LYS184 | |
B | PHE82 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1b9h |
Chain | Residue | Details |
A | ASP155 | |
A | PHE82 |