6RGT
Crystal structure of the cofactor-free Aspergillus flavus urate oxidase T57A variant anaerobically complexed with 9-methyl uric acid
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004846 | molecular_function | urate oxidase activity |
A | 0005777 | cellular_component | peroxisome |
A | 0006144 | biological_process | purine nucleobase metabolic process |
A | 0006145 | biological_process | purine nucleobase catabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0019628 | biological_process | urate catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | binding site for residue MUA A 401 |
Chain | Residue |
A | TYR8 |
A | GLN228 |
A | ASN254 |
A | HOH583 |
A | HOH592 |
A | HOH794 |
A | HOH953 |
A | ALA56 |
A | ALA57 |
A | ASP58 |
A | PHE159 |
A | LEU170 |
A | ARG176 |
A | SER226 |
A | VAL227 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue MPD A 402 |
Chain | Residue |
A | GLN158 |
A | TRP160 |
A | TRP174 |
A | HOH515 |
A | HOH654 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue TRS A 403 |
Chain | Residue |
A | VAL3 |
A | LYS4 |
A | GLY40 |
A | ILE42 |
A | GLU43 |
A | HOH523 |
A | HOH685 |
A | HOH715 |
A | HOH720 |
site_id | AC4 |
Number of Residues | 8 |
Details | binding site for residue TRS A 404 |
Chain | Residue |
A | ASP11 |
A | ASN12 |
A | THR33 |
A | CYS35 |
A | ASN100 |
A | VAL102 |
A | HOH556 |
A | HOH699 |
Functional Information from PROSITE/UniProt
site_id | PS00366 |
Number of Residues | 28 |
Details | URICASE Uricase signature. LtVLKSTnSqFwgFlrdeYttLketwdR |
Chain | Residue | Details |
A | LEU149-ARG176 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | ACT_SITE: Charge relay system => ECO:0000269|PubMed:24466188, ECO:0007744|PDB:4N3M, ECO:0007744|PDB:4N9M, ECO:0007744|PDB:4N9S, ECO:0007744|PDB:4N9V |
Chain | Residue | Details |
A | LYS10 | |
A | ALA57 | |
A | HIS256 |
Chain | Residue | Details |
A | ALA57 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000305|PubMed:9360612, ECO:0007744|PDB:1R4S, ECO:0007744|PDB:3LBG, ECO:0007744|PDB:3LD4, ECO:0007744|PDB:4CW0, ECO:0007744|PDB:4CW2, ECO:0007744|PDB:4CW3, ECO:0007744|PDB:4CW6, ECO:0007744|PDB:4N9S |
Chain | Residue | Details |
A | ASP58 |
Chain | Residue | Details |
A | PHE159 |
Chain | Residue | Details |
A | ARG176 |
Chain | Residue | Details |
A | VAL227 |
Chain | Residue | Details |
A | GLN228 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0007744|PDB:4CW2, ECO:0007744|PDB:4CW3, ECO:0007744|PDB:4CW6 |
Chain | Residue | Details |
A | ASN254 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylserine => ECO:0000305|PubMed:1339455, ECO:0007744|PDB:1R4S, ECO:0007744|PDB:1R4U, ECO:0007744|PDB:1R51, ECO:0007744|PDB:1R56, ECO:0007744|PDB:1WRR, ECO:0007744|PDB:1WS2, ECO:0007744|PDB:1WS3, ECO:0007744|PDB:1XT4, ECO:0007744|PDB:1XXJ, ECO:0007744|PDB:1XY3, ECO:0007744|PDB:2FXL, ECO:0007744|PDB:3BJP, ECO:0007744|PDB:4FSK |
Chain | Residue | Details |
A | SER1 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 118 |
Chain | Residue | Details |
A | LYS10 | hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | ALA57 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | ARG176 | electrostatic stabiliser |
A | GLN228 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
A | HIS256 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |