1FIQ
CRYSTAL STRUCTURE OF XANTHINE OXIDASE FROM BOVINE MILK
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0071949 | molecular_function | FAD binding |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0043546 | molecular_function | molybdopterin cofactor binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES A 601 |
| Chain | Residue |
| A | GLN112 |
| A | CYS113 |
| A | GLY114 |
| A | CYS116 |
| A | CYS148 |
| A | ARG149 |
| A | CYS150 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE FES A 602 |
| Chain | Residue |
| A | GLY44 |
| A | GLY46 |
| A | GLY47 |
| A | CYS48 |
| A | GLY49 |
| A | CYS51 |
| A | ASN71 |
| A | CYS73 |
| A | GLY42 |
| A | CYS43 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE MTE C 1333 |
| Chain | Residue |
| A | GLN112 |
| A | CYS150 |
| C | GLY796 |
| C | GLY797 |
| C | PHE798 |
| C | ARG912 |
| C | MET1038 |
| C | GLY1039 |
| C | GLN1040 |
| C | ALA1078 |
| C | ALA1079 |
| C | SER1080 |
| C | VAL1081 |
| C | SER1082 |
| C | GLN1194 |
| C | GLU1261 |
| C | MOS1334 |
| C | HOH1433 |
| C | HOH1516 |
| C | HOH1601 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MOS C 1334 |
| Chain | Residue |
| C | GLN767 |
| C | PHE798 |
| C | GLY799 |
| C | PHE911 |
| C | ARG912 |
| C | ALA1078 |
| C | ALA1079 |
| C | GLU1261 |
| C | MTE1333 |
| C | SAL1335 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SAL C 1335 |
| Chain | Residue |
| C | GLU802 |
| C | ARG880 |
| C | PHE914 |
| C | SER1008 |
| C | PHE1009 |
| C | THR1010 |
| C | VAL1011 |
| C | MOS1334 |
| C | HOH1457 |
| site_id | AC6 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FAD B 606 |
| Chain | Residue |
| A | GLU45 |
| A | GLY46 |
| B | LYS256 |
| B | LEU257 |
| B | VAL258 |
| B | VAL259 |
| B | GLY260 |
| B | ASN261 |
| B | THR262 |
| B | GLU263 |
| B | ILE264 |
| B | LEU287 |
| B | PHE337 |
| B | ALA338 |
| B | ALA346 |
| B | SER347 |
| B | GLY350 |
| B | ASN351 |
| B | ILE353 |
| B | THR354 |
| B | SER359 |
| B | ASP360 |
| B | LEU404 |
| B | HOH714 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL C 1336 |
| Chain | Residue |
| C | ARG839 |
| C | HIS840 |
| C | ILE877 |
| C | THR909 |
| C | ALA910 |
| C | PHE911 |
| C | PHE914 |
| C | GLY915 |
| C | GLN918 |
Functional Information from PROSITE/UniProt
| site_id | PS00197 |
| Number of Residues | 9 |
| Details | 2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CGEGGCGAC |
| Chain | Residue | Details |
| A | CYS43-CYS51 |
| site_id | PS00559 |
| Number of Residues | 36 |
| Details | MOLYBDOPTERIN_EUK Eukaryotic molybdopterin oxidoreductases signature. GFggKetrstlvsvava..LaayKTghpVrCmlDRneD |
| Chain | Residue | Details |
| C | GLY797-ASP832 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 87 |
| Details | Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12421831","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15148401","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19109252","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 185 |
| Details | Domain: {"description":"FAD-binding PCMH-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00718","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 15 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12421831","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15148401","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"15148401","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 19109252, 15148401 |
| Chain | Residue | Details |
| C | GLU1261 | |
| C | ARG880 | |
| C | GLU802 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 139 |
| Chain | Residue | Details |
| C | GLU802 | electrostatic stabiliser, hydrogen bond acceptor |
| C | ARG880 | electrostatic stabiliser, hydrogen bond donor |
| C | GLU1261 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
