Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0008483 | molecular_function | transaminase activity |
A | 0009102 | biological_process | biotin biosynthetic process |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0008483 | molecular_function | transaminase activity |
B | 0009102 | biological_process | biotin biosynthetic process |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 18 |
Details | binding site for residue PLP A 501 |
Chain | Residue |
A | GLY124 |
A | LYS283 |
A | 3GS502 |
A | HOH643 |
A | HOH648 |
A | HOH650 |
A | HOH686 |
A | HOH698 |
B | PRO317 |
B | THR318 |
A | SER125 |
A | TYR157 |
A | HIS158 |
A | GLY159 |
A | GLU220 |
A | ASP254 |
A | ILE256 |
A | ALA257 |
site_id | AC2 |
Number of Residues | 13 |
Details | binding site for residue 3GS A 502 |
Chain | Residue |
A | PRO24 |
A | TYR25 |
A | TRP64 |
A | TYR157 |
A | ARG400 |
A | PHE402 |
A | PLP501 |
A | HOH686 |
B | MET91 |
B | GLY93 |
B | GLY316 |
B | PRO317 |
B | THR318 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue PEG A 503 |
Chain | Residue |
A | HIS232 |
A | PRO234 |
A | HIS271 |
A | HOH733 |
site_id | AC4 |
Number of Residues | 16 |
Details | binding site for residue PLP B 501 |
Chain | Residue |
A | THR318 |
A | HOH644 |
B | GLY124 |
B | SER125 |
B | TYR157 |
B | HIS158 |
B | GLU220 |
B | ASP254 |
B | ILE256 |
B | ALA257 |
B | LYS283 |
B | 3GS502 |
B | HOH659 |
B | HOH662 |
B | HOH666 |
B | HOH674 |
site_id | AC5 |
Number of Residues | 13 |
Details | binding site for residue 3GS B 502 |
Chain | Residue |
A | MET91 |
A | PHE92 |
A | GLY93 |
A | GLY316 |
A | PRO317 |
A | THR318 |
B | PRO24 |
B | TYR25 |
B | TRP64 |
B | TYR157 |
B | ARG400 |
B | PLP501 |
B | HOH662 |
site_id | AC6 |
Number of Residues | 8 |
Details | binding site for residue EDO B 503 |
Chain | Residue |
B | THR152 |
B | TRP153 |
B | GLY156 |
B | HIS158 |
B | ILE167 |
B | VAL219 |
B | GLU220 |
B | GLN224 |
site_id | AC7 |
Number of Residues | 1 |
Details | binding site for residue EDO B 505 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue EDO B 506 |
Chain | Residue |
B | LEU337 |
B | GLN339 |
B | ASP340 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue EDO B 507 |
Chain | Residue |
A | HIS271 |
B | ARG246 |
B | TYR247 |
B | HOH601 |
Functional Information from PROSITE/UniProt
site_id | PS00600 |
Number of Residues | 38 |
Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIfDEIat.GFgRtGalfaadhagvsp....DIMcvGKaltGG |
Chain | Residue | Details |
A | LEU251-GLY288 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | TRP64 | |
B | GLY124 | |
B | TYR157 | |
B | ASP254 | |
B | LYS283 | |
B | GLY316 | |
B | PRO317 | |
B | ARG400 | |
A | GLY124 | |
A | TYR157 | |
A | ASP254 | |
A | LYS283 | |
A | GLY316 | |
A | PRO317 | |
A | ARG400 | |
B | TRP64 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM => ECO:0000250 |
Chain | Residue | Details |
A | TYR25 | |
B | TYR25 | |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
Chain | Residue | Details |
A | LYS283 | |
B | LYS283 | |