3QN6
Crystal Structures of Escherichia coli Aspartate Aminotransferase Reconstituted with 1-Deaza-Pyridoxal 5'-Phosphate: Internal Aldimine and Stable L-Aspartate External Aldimine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
A | 0004838 | molecular_function | L-tyrosine:2-oxoglutarate aminotransferase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006520 | biological_process | amino acid metabolic process |
A | 0008483 | molecular_function | transaminase activity |
A | 0009058 | biological_process | biosynthetic process |
A | 0009094 | biological_process | L-phenylalanine biosynthetic process |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0033585 | biological_process | L-phenylalanine biosynthetic process from chorismate via phenylpyruvate |
A | 0042802 | molecular_function | identical protein binding |
A | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 409 |
Chain | Residue |
A | ARG327 |
A | GLN328 |
A | HOH527 |
A | HOH786 |
A | HOH797 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 410 |
Chain | Residue |
A | HOH11 |
A | PRO84 |
A | ARG88 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 411 |
Chain | Residue |
A | ARG134 |
A | ARG372 |
A | ALA406 |
A | HOH537 |
A | LYS133 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 412 |
Chain | Residue |
A | ARG108 |
A | LYS288 |
A | HOH477 |
A | HOH536 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 413 |
Chain | Residue |
A | LYS146 |
A | ASN150 |
A | GLU155 |
A | VAL156 |
A | ARG157 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 414 |
Chain | Residue |
A | GLY232 |
A | LEU233 |
A | GLU234 |
A | GLU235 |
A | HOH562 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO A 415 |
Chain | Residue |
A | PRO84 |
A | GLY87 |
A | ARG88 |
A | GLN91 |
A | ARG108 |
A | THR109 |
A | HOH445 |
A | HOH548 |
A | HOH564 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A 416 |
Chain | Residue |
A | GLU65 |
A | GLU65 |
A | LEU68 |
A | LEU69 |
A | GLU72 |
A | LYS75 |
A | HIS301 |
A | HOH455 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 417 |
Chain | Residue |
A | TYR48 |
A | PRO56 |
A | 3QN258 |
A | GLY261 |
A | TYR263 |
A | HOH752 |
Functional Information from PROSITE/UniProt
site_id | PS00105 |
Number of Residues | 14 |
Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SYSKnfGLyNERVG |
Chain | Residue | Details |
A | SER255-GLY268 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC |
Chain | Residue | Details |
A | GLY46 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0007744|PDB:1AIB, ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:1SPA, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC |
Chain | Residue | Details |
A | TRP142 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0007744|PDB:1AIB, ECO:0007744|PDB:1ART, ECO:0007744|PDB:1ASC, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:1SPA, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC |
Chain | Residue | Details |
A | ASN195 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0007744|PDB:1AHG, ECO:0007744|PDB:1AIB, ECO:0007744|PDB:1ARG, ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC |
Chain | Residue | Details |
A | ARG386 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:11148029, ECO:0000269|PubMed:1993208, ECO:0000269|PubMed:3298240, ECO:0000269|PubMed:9891001, ECO:0007744|PDB:1AAW, ECO:0007744|PDB:1AHE, ECO:0007744|PDB:1AHF, ECO:0007744|PDB:1AHX, ECO:0007744|PDB:1AHY, ECO:0007744|PDB:1ARI, ECO:0007744|PDB:1ARS, ECO:0007744|PDB:1ASA, ECO:0007744|PDB:1ASB, ECO:0007744|PDB:1ASD, ECO:0007744|PDB:1ASE, ECO:0007744|PDB:1ASF, ECO:0007744|PDB:1ASG, ECO:0007744|PDB:1ASM, ECO:0007744|PDB:1ASN, ECO:0007744|PDB:1B4X, ECO:0007744|PDB:1CZC, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:1G4V, ECO:0007744|PDB:1G4X, ECO:0007744|PDB:1G7W, ECO:0007744|PDB:1G7X, ECO:0007744|PDB:1IX6, ECO:0007744|PDB:1IX7, ECO:0007744|PDB:1IX8, ECO:0007744|PDB:1QIR, ECO:0007744|PDB:1QIS, ECO:0007744|PDB:1QIT, ECO:0007744|PDB:1YOO, ECO:0007744|PDB:2D5Y, ECO:0007744|PDB:2D61, ECO:0007744|PDB:2D63, ECO:0007744|PDB:2D7Y, ECO:0007744|PDB:3AAT, ECO:0007744|PDB:3ZZJ, ECO:0007744|PDB:5EAA |
Chain | Residue | Details |
A | 3QN258 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 777 |
Chain | Residue | Details |
A | TRP142 | steric role |
A | ASP223 | proton shuttle (general acid/base) |
A | 3QN258 | proton shuttle (general acid/base) |