4BQ0
Pseudomonas aeruginosa beta-alanine:pyruvate aminotransferase holoenzyme without divalent cations on dimer-dimer interface
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
A | 0008483 | molecular_function | transaminase activity |
A | 0009102 | biological_process | biotin biosynthetic process |
A | 0016223 | molecular_function | beta-alanine-pyruvate transaminase activity |
A | 0019483 | biological_process | beta-alanine biosynthetic process |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
B | 0008483 | molecular_function | transaminase activity |
B | 0009102 | biological_process | biotin biosynthetic process |
B | 0016223 | molecular_function | beta-alanine-pyruvate transaminase activity |
B | 0019483 | biological_process | beta-alanine biosynthetic process |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
C | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
C | 0008483 | molecular_function | transaminase activity |
C | 0009102 | biological_process | biotin biosynthetic process |
C | 0016223 | molecular_function | beta-alanine-pyruvate transaminase activity |
C | 0019483 | biological_process | beta-alanine biosynthetic process |
C | 0030170 | molecular_function | pyridoxal phosphate binding |
D | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
D | 0008483 | molecular_function | transaminase activity |
D | 0009102 | biological_process | biotin biosynthetic process |
D | 0016223 | molecular_function | beta-alanine-pyruvate transaminase activity |
D | 0019483 | biological_process | beta-alanine biosynthetic process |
D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 1449 |
Chain | Residue |
A | PHE322 |
A | SER323 |
A | HOH2459 |
B | MET172 |
B | PHE173 |
site_id | AC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE PLP A 1450 |
Chain | Residue |
A | HIS154 |
A | GLY155 |
A | GLU226 |
A | ASP259 |
A | VAL261 |
A | ILE262 |
A | LYS288 |
A | HOH2270 |
A | HOH2382 |
A | HOH2435 |
A | HOH2557 |
B | TYR326 |
B | THR327 |
A | SER119 |
A | GLY120 |
A | SER121 |
A | TYR153 |
site_id | AC3 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE PLP B 1449 |
Chain | Residue |
A | TYR326 |
A | THR327 |
A | HOH2462 |
A | HOH2463 |
B | SER119 |
B | GLY120 |
B | SER121 |
B | TYR153 |
B | HIS154 |
B | GLY155 |
B | GLU226 |
B | ASP259 |
B | VAL261 |
B | ILE262 |
B | LYS288 |
B | HOH2291 |
B | HOH2337 |
site_id | AC4 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE PLP C 1449 |
Chain | Residue |
C | SER119 |
C | GLY120 |
C | SER121 |
C | TYR153 |
C | HIS154 |
C | GLY155 |
C | GLU226 |
C | ASP259 |
C | VAL261 |
C | ILE262 |
C | LYS288 |
C | HOH2178 |
C | HOH2247 |
C | HOH2286 |
C | HOH2378 |
D | TYR326 |
D | THR327 |
site_id | AC5 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE PLP D 1449 |
Chain | Residue |
C | TYR326 |
C | THR327 |
C | HOH2306 |
C | HOH2307 |
D | SER119 |
D | GLY120 |
D | SER121 |
D | TYR153 |
D | HIS154 |
D | GLY155 |
D | GLU226 |
D | ASP259 |
D | VAL261 |
D | ILE262 |
D | LYS288 |
D | HOH2184 |
D | HOH2229 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL B 1450 |
Chain | Residue |
A | MET172 |
A | PHE173 |
A | HOH2283 |
B | PHE322 |
B | SER323 |
B | HOH2353 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL C 1450 |
Chain | Residue |
C | PHE322 |
C | SER323 |
C | HOH2302 |
C | HOH2305 |
D | PHE173 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL D 1450 |
Chain | Residue |
C | MET172 |
C | PHE173 |
C | HOH2189 |
D | SER323 |
Functional Information from PROSITE/UniProt
site_id | PS00600 |
Number of Residues | 38 |
Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIfDEVit.AFgRlGtysgaeyfgvtp....DLMnvAKqvtNG |
Chain | Residue | Details |
A | LEU256-GLY293 |
site_id | PS00639 |
Number of Residues | 11 |
Details | THIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. GYHGVNVAGTS |
Chain | Residue | Details |
A | GLY152-SER162 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23519665 |
Chain | Residue | Details |
A | TRP61 | |
D | TRP61 | |
D | ARG414 | |
D | GLN421 | |
A | ARG414 | |
A | GLN421 | |
B | TRP61 | |
B | ARG414 | |
B | GLN421 | |
C | TRP61 | |
C | ARG414 | |
C | GLN421 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY120 | |
B | GLY120 | |
C | GLY120 | |
D | GLY120 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23519665, ECO:0000269|Ref.4 |
Chain | Residue | Details |
A | THR327 | |
B | THR327 | |
C | THR327 | |
D | THR327 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
Chain | Residue | Details |
A | LYS288 | |
B | LYS288 | |
C | LYS288 | |
D | LYS288 |