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 | 13 |
Details | BINDING SITE FOR RESIDUE PLP A 500 |
Chain | Residue |
A | GLY106 |
A | SER246 |
A | LYS247 |
A | ARG255 |
B | TYR71 |
A | ALA107 |
A | ALA108 |
A | PHE133 |
A | ASN178 |
A | ASN182 |
A | ASP216 |
A | TYR219 |
A | SER244 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PLP B 500 |
Chain | Residue |
A | TYR71 |
B | GLY106 |
B | ALA107 |
B | ALA108 |
B | PHE133 |
B | ASN178 |
B | ASN182 |
B | ASP216 |
B | TYR219 |
B | SER244 |
B | SER246 |
B | LYS247 |
B | ARG255 |
B | HOH611 |
site_id | AC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PLP C 500 |
Chain | Residue |
C | GLY106 |
C | ALA107 |
C | ALA108 |
C | PHE133 |
C | ASN178 |
C | ASN182 |
C | ASP216 |
C | TYR219 |
C | SER244 |
C | SER246 |
C | LYS247 |
C | ARG255 |
D | TYR71 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PLP D 500 |
Chain | Residue |
C | TYR71 |
D | GLY106 |
D | ALA107 |
D | ALA108 |
D | ASN178 |
D | ASN182 |
D | ASP216 |
D | TYR219 |
D | SER244 |
D | SER246 |
D | LYS247 |
D | ARG255 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL B 501 |
Chain | Residue |
B | ASN141 |
B | ARG146 |
B | LEU147 |
B | EDO510 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL D 501 |
Chain | Residue |
D | LYS137 |
D | ASN141 |
D | ARG146 |
D | LEU147 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 501 |
Chain | Residue |
A | TYR243 |
A | GLN299 |
A | GLY300 |
A | ALA301 |
A | THR302 |
A | HOH705 |
A | HOH969 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO B 502 |
Chain | Residue |
A | HOH737 |
A | HOH868 |
B | GLU221 |
B | TYR243 |
B | GLN299 |
B | GLY300 |
B | ALA301 |
B | THR302 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO C 501 |
Chain | Residue |
C | PHE87 |
C | TYR243 |
C | SER248 |
C | GLY300 |
C | ALA301 |
C | THR302 |
C | HOH776 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 503 |
Chain | Residue |
A | HOH598 |
A | HOH771 |
B | SER204 |
B | ARG209 |
B | PRO210 |
B | HOH617 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 502 |
Chain | Residue |
A | TYR23 |
A | ARG27 |
A | GLU353 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 504 |
Chain | Residue |
B | GLU125 |
B | ARG146 |
B | HOH578 |
B | HOH597 |
B | HOH602 |
C | ARG146 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 505 |
Chain | Residue |
B | VAL376 |
B | ASP377 |
B | ARG378 |
B | SER45 |
B | ASN311 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 506 |
Chain | Residue |
B | GLY42 |
B | PHE133 |
B | ASN182 |
B | TYR334 |
B | ARG371 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO B 507 |
Chain | Residue |
A | HOH561 |
B | ALA170 |
site_id | BC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 508 |
Chain | Residue |
A | TYR8 |
B | ASP267 |
B | GLU270 |
B | PRO386 |
B | GLU389 |
B | LYS393 |
site_id | BC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 509 |
Chain | Residue |
B | LYS137 |
B | LEU147 |
B | GLU149 |
site_id | BC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 510 |
Chain | Residue |
B | LYS137 |
B | ASN141 |
B | ARG146 |
B | CL501 |
C | TYR123 |
C | HIS171 |
Functional Information from PROSITE/UniProt
site_id | PS00105 |
Number of Residues | 14 |
Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SYSKslSLpGERIG |
Chain | Residue | Details |
A | SER244-GLY257 | |