Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005575 | cellular_component | cellular_component |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0008483 | molecular_function | transaminase activity |
A | 0016829 | molecular_function | lyase activity |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0050459 | molecular_function | ethanolamine-phosphate phospho-lyase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005575 | cellular_component | cellular_component |
B | 0005739 | cellular_component | mitochondrion |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0008483 | molecular_function | transaminase activity |
B | 0016829 | molecular_function | lyase activity |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0050459 | molecular_function | ethanolamine-phosphate phospho-lyase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | binding site for residue GOL A 501 |
Chain | Residue |
A | VAL66 |
A | GLY281 |
A | ASN282 |
A | HIS284 |
A | HOH652 |
B | MET74 |
B | ASN78 |
B | HIS284 |
B | VAL315 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue GOL A 502 |
Chain | Residue |
A | TYR40 |
A | GLN48 |
A | LEU50 |
A | ARG396 |
A | PHE424 |
A | HOH654 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue GOL A 503 |
Chain | Residue |
A | GLU328 |
A | GLN333 |
A | HOH666 |
A | HOH694 |
site_id | AC4 |
Number of Residues | 13 |
Details | binding site for residue PMP A 504 |
Chain | Residue |
A | SER111 |
A | GLY112 |
A | SER113 |
A | ASN116 |
A | TYR139 |
A | HIS140 |
A | HIS142 |
A | ASP246 |
A | VAL248 |
A | GLN249 |
A | LYS278 |
A | HOH602 |
A | HOH631 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue GOL B 501 |
Chain | Residue |
A | MET74 |
A | ASN78 |
B | VAL66 |
B | GLY281 |
B | HIS284 |
B | HOH667 |
B | HOH782 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue GOL B 502 |
Chain | Residue |
B | GLN48 |
B | LEU50 |
B | ARG396 |
B | PHE424 |
B | HOH611 |
B | HOH642 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue GOL B 503 |
Chain | Residue |
B | GLU328 |
B | GLN333 |
B | HOH648 |
B | HOH799 |
site_id | AC8 |
Number of Residues | 12 |
Details | binding site for residue PMP B 504 |
Chain | Residue |
B | SER111 |
B | GLY112 |
B | SER113 |
B | ASN116 |
B | TYR139 |
B | HIS140 |
B | HIS142 |
B | ASP246 |
B | GLN249 |
B | LYS278 |
B | HOH601 |
B | HOH638 |
Functional Information from PROSITE/UniProt
site_id | PS00600 |
Number of Residues | 41 |
Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. FIaDEVqv.GFgRvGkhfwsfqmygedfvp.DIVtmGKpmgNG |
Chain | Residue | Details |
A | PHE243-GLY283 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
Chain | Residue | Details |
A | LYS278 | |
B | LYS278 | |