2PES
Urate Oxidase in complex with tris-dipicolinate Lutetium
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 | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE AZA A 300 |
Chain | Residue |
A | ILE54 |
A | ALA56 |
A | THR57 |
A | PHE159 |
A | ARG176 |
A | SER226 |
A | GLN228 |
A | ASN254 |
A | HOH324 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PDC A 302 |
Chain | Residue |
A | PRO202 |
A | LYS203 |
A | ALA206 |
A | GLN242 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PDC A 303 |
Chain | Residue |
A | SER199 |
A | HIS200 |
A | PRO202 |
A | LYS203 |
A | HOH480 |
site_id | AC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE PDC A 304 |
Chain | Residue |
A | HOH477 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PDC A 305 |
Chain | Residue |
A | ARG164 |
A | HOH411 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PDC A 306 |
Chain | Residue |
A | ARG164 |
A | ASP165 |
A | THR168 |
site_id | AC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE PDC A 307 |
Chain | Residue |
A | HOH477 |
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 | THR57 | |
A | HIS256 |
Chain | Residue | Details |
A | THR57 |
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 | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1r51 |
Chain | Residue | Details |
A | GLN228 | |
A | ARG176 |
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 | THR57 | 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 |