Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0008483 | molecular_function | transaminase activity |
A | 0009058 | biological_process | biosynthetic process |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0008483 | molecular_function | transaminase activity |
B | 0009058 | biological_process | biosynthetic process |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0008483 | molecular_function | transaminase activity |
C | 0009058 | biological_process | biosynthetic process |
C | 0030170 | molecular_function | pyridoxal phosphate binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0008483 | molecular_function | transaminase activity |
D | 0009058 | biological_process | biosynthetic process |
D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 338 |
Chain | Residue |
A | ARG258 |
A | ARG265 |
A | SER273 |
A | EDO346 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE TLA A 343 |
Chain | Residue |
A | PHE306 |
A | ARG313 |
A | HOH897 |
A | HOH908 |
B | TYR47 |
A | PHE22 |
A | ASN145 |
A | TYR172 |
A | LYS197 |
A | LYS301 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 346 |
Chain | Residue |
A | ARG257 |
A | ARG258 |
A | SER274 |
A | SO4338 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 349 |
Chain | Residue |
A | ASN69 |
A | SER213 |
A | GLU214 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 350 |
Chain | Residue |
A | ALA285 |
A | GLU287 |
A | ARG288 |
A | HOH677 |
A | HOH829 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 339 |
Chain | Residue |
B | ARG258 |
B | ARG265 |
B | SER273 |
B | TLA342 |
B | HOH916 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 340 |
Chain | Residue |
B | ASN145 |
B | LYS301 |
B | ARG313 |
B | HOH909 |
B | HOH911 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE TLA B 342 |
Chain | Residue |
B | ARG257 |
B | ARG258 |
B | ALA261 |
B | SER273 |
B | SER274 |
B | GLU275 |
B | SO4339 |
B | HOH916 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 347 |
Chain | Residue |
B | ASN283 |
B | GLY286 |
B | ASP302 |
B | HIS309 |
B | HIS310 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO B 351 |
Chain | Residue |
A | GLU115 |
B | SER64 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 353 |
Chain | Residue |
B | ILE76 |
B | PHE99 |
B | ASN145 |
B | ASP169 |
B | THR171 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 356 |
Chain | Residue |
B | ALA285 |
B | GLU287 |
B | ARG288 |
B | ARG291 |
site_id | BC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE TLA C 344 |
Chain | Residue |
C | PHE22 |
C | ASN145 |
C | LYS197 |
C | ARG205 |
C | LYS301 |
C | PHE306 |
C | ARG313 |
C | HOH913 |
C | HOH915 |
D | TYR47 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE TLA C 345 |
Chain | Residue |
C | ARG257 |
C | ARG258 |
C | ARG265 |
C | SER273 |
C | SER274 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO C 348 |
Chain | Residue |
C | GLY286 |
C | GLU287 |
C | LEU290 |
C | ASP302 |
C | HIS309 |
C | HIS310 |
site_id | BC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO C 352 |
site_id | BC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO C 357 |
Chain | Residue |
C | ALA285 |
C | GLU287 |
C | ARG288 |
C | HIS310 |
C | HOH870 |
D | ARG54 |
D | LYS58 |
D | GLU237 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 D 337 |
Chain | Residue |
D | ARG258 |
D | ARG265 |
D | SER273 |
D | TLA341 |
site_id | CC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE TLA D 341 |
Chain | Residue |
D | SO4337 |
D | ARG257 |
D | ARG258 |
D | SER273 |
D | SER274 |
D | GLU275 |
site_id | CC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO D 354 |
Chain | Residue |
D | PHE99 |
D | ASN145 |
D | ASP169 |
D | THR171 |
site_id | CC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO D 358 |
Chain | Residue |
D | ALA285 |
D | GLU287 |
D | ARG288 |
D | ARG291 |
Functional Information from PROSITE/UniProt
site_id | PS00105 |
Number of Residues | 14 |
Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SFSKsyGLaGLRLG |
Chain | Residue | Details |
A | SER194-GLY207 | |