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 | 17 |
Details | binding site for residue PLP A 501 |
Chain | Residue |
A | TRP65 |
A | 3VR502 |
A | HOH622 |
A | HOH737 |
A | HOH741 |
A | HOH784 |
B | GLY316 |
B | PRO317 |
B | THR318 |
A | SER125 |
A | TYR157 |
A | HIS158 |
A | GLU220 |
A | ASP254 |
A | ILE256 |
A | ALA257 |
A | LYS283 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue 3VR A 502 |
Chain | Residue |
A | TYR25 |
A | TRP64 |
A | TRP65 |
A | TYR157 |
A | MET174 |
A | ALA226 |
A | PLP501 |
A | EPE503 |
A | HOH644 |
B | GLY316 |
B | THR318 |
site_id | AC3 |
Number of Residues | 11 |
Details | binding site for residue EPE A 503 |
Chain | Residue |
A | TYR25 |
A | SER27 |
A | GLU31 |
A | TRP64 |
A | ARG400 |
A | 3VR502 |
A | HOH676 |
A | HOH707 |
A | HOH714 |
B | GLY93 |
B | GLY94 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue EDO A 504 |
Chain | Residue |
A | ARG193 |
A | ARG230 |
A | PHE231 |
A | ARG369 |
A | HOH612 |
A | HOH860 |
A | HOH917 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue EDO A 505 |
Chain | Residue |
A | PRO234 |
A | CYS371 |
A | HOH611 |
A | HOH890 |
site_id | AC6 |
Number of Residues | 9 |
Details | binding site for residue EDO A 506 |
Chain | Residue |
A | ARG142 |
A | LEU144 |
A | HOH615 |
A | HOH641 |
A | HOH812 |
B | ARG154 |
B | GLN185 |
B | VAL186 |
B | PHE187 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue EDO A 507 |
Chain | Residue |
A | GLY355 |
A | THR358 |
A | THR423 |
A | SER424 |
A | HOH620 |
B | ARG85 |
B | HOH829 |
B | HOH935 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue EDO A 508 |
Chain | Residue |
A | ARG241 |
A | ARG245 |
A | HOH638 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue EDO A 509 |
Chain | Residue |
A | ILE110 |
A | THR111 |
A | PRO112 |
A | ALA113 |
A | ASP270 |
A | EDO510 |
B | ARG235 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue EDO A 510 |
Chain | Residue |
A | ASP270 |
A | EDO509 |
B | ARG235 |
B | HIS238 |
site_id | AD2 |
Number of Residues | 11 |
Details | binding site for residue 3VR B 502 |
Chain | Residue |
A | GLY316 |
A | THR318 |
B | TYR25 |
B | TRP64 |
B | TRP65 |
B | TYR157 |
B | ALA226 |
B | PHE402 |
B | PLP501 |
B | EPE503 |
B | HOH634 |
site_id | AD3 |
Number of Residues | 11 |
Details | binding site for residue EPE B 503 |
Chain | Residue |
B | 3VR502 |
B | HOH660 |
B | HOH683 |
B | HOH729 |
A | GLY93 |
A | GLY94 |
B | TYR25 |
B | SER27 |
B | GLU31 |
B | TRP64 |
B | ARG400 |
site_id | AD4 |
Number of Residues | 8 |
Details | binding site for residue EDO B 504 |
Chain | Residue |
A | ARG403 |
A | ASN404 |
B | GLN53 |
B | ILE55 |
B | HOH687 |
B | HOH734 |
B | HOH809 |
B | HOH851 |
site_id | AD5 |
Number of Residues | 6 |
Details | binding site for residue EDO B 505 |
Chain | Residue |
B | ARG193 |
B | ARG230 |
B | PHE231 |
B | ARG369 |
B | HOH614 |
B | HOH684 |
site_id | AD6 |
Number of Residues | 2 |
Details | binding site for residue EDO B 506 |
site_id | AD7 |
Number of Residues | 2 |
Details | binding site for residue EDO B 507 |
Chain | Residue |
B | ARG193 |
B | ASP194 |
site_id | AD8 |
Number of Residues | 25 |
Details | binding site for Di-peptide PLP B 501 and LYS B 283 |
Chain | Residue |
A | GLY316 |
A | PRO317 |
A | THR318 |
A | PHE319 |
B | TRP64 |
B | TRP65 |
B | GLY124 |
B | SER125 |
B | TYR157 |
B | HIS158 |
B | GLU220 |
B | ASP254 |
B | ILE256 |
B | ALA257 |
B | GLY282 |
B | ALA284 |
B | LEU285 |
B | THR286 |
B | 3VR502 |
B | HOH616 |
B | HOH669 |
B | HOH704 |
B | HOH708 |
B | HOH761 |
B | HOH817 |
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
Chain | Residue | Details |
A | TRP64 | |
A | TYR157 | |
A | GLY316 | |
B | TRP64 | |
B | TYR157 | |
B | GLY316 | |
Chain | Residue | Details |
A | GLY124 | |
A | ASP254 | |
A | LYS283 | |
A | PRO317 | |
B | GLY124 | |
B | ASP254 | |
B | LYS283 | |
B | PRO317 | |
Chain | Residue | Details |
A | ARG400 | |
B | ARG400 | |
site_id | SWS_FT_FI4 |
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:0000305|PubMed:20565114 |
Chain | Residue | Details |
A | TYR25 | |
B | TYR25 | |
Chain | Residue | Details |
A | LYS283 | |
B | LYS283 | |