3EUB
Crystal Structure of Desulfo-Xanthine Oxidase with Xanthine
Functional Information from GO Data
Chain | GOid | namespace | contents |
2 | 0005506 | molecular_function | iron ion binding |
2 | 0016491 | molecular_function | oxidoreductase activity |
2 | 0046872 | molecular_function | metal ion binding |
2 | 0051536 | molecular_function | iron-sulfur cluster binding |
2 | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
3 | 0005506 | molecular_function | iron ion binding |
3 | 0016491 | molecular_function | oxidoreductase activity |
3 | 0050660 | molecular_function | flavin adenine dinucleotide binding |
3 | 0071949 | molecular_function | FAD binding |
4 | 0005506 | molecular_function | iron ion binding |
4 | 0016491 | molecular_function | oxidoreductase activity |
4 | 0043546 | molecular_function | molybdopterin cofactor binding |
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 |
J | 0005506 | molecular_function | iron ion binding |
J | 0016491 | molecular_function | oxidoreductase activity |
J | 0046872 | molecular_function | metal ion binding |
J | 0051536 | molecular_function | iron-sulfur cluster binding |
J | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
K | 0005506 | molecular_function | iron ion binding |
K | 0016491 | molecular_function | oxidoreductase activity |
K | 0050660 | molecular_function | flavin adenine dinucleotide binding |
K | 0071949 | molecular_function | FAD binding |
L | 0005506 | molecular_function | iron ion binding |
L | 0016491 | molecular_function | oxidoreductase activity |
L | 0043546 | molecular_function | molybdopterin cofactor binding |
S | 0005506 | molecular_function | iron ion binding |
S | 0016491 | molecular_function | oxidoreductase activity |
S | 0046872 | molecular_function | metal ion binding |
S | 0051536 | molecular_function | iron-sulfur cluster binding |
S | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
T | 0005506 | molecular_function | iron ion binding |
T | 0016491 | molecular_function | oxidoreductase activity |
T | 0050660 | molecular_function | flavin adenine dinucleotide binding |
T | 0071949 | molecular_function | FAD binding |
U | 0005506 | molecular_function | iron ion binding |
U | 0016491 | molecular_function | oxidoreductase activity |
U | 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 | 15 |
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 | SER1082 |
C | GLN1194 |
C | MOM1334 |
site_id | AC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE MOM C 1334 |
Chain | Residue |
C | GLN767 |
C | PHE798 |
C | GLY799 |
C | GLU802 |
C | PHE911 |
C | ARG912 |
C | ALA1078 |
C | ALA1079 |
C | GLU1261 |
C | MTE1333 |
C | XAN7319 |
site_id | AC5 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE FAD B 606 |
Chain | Residue |
A | GLY46 |
B | LYS256 |
B | LEU257 |
B | VAL258 |
B | VAL259 |
B | GLY260 |
B | ASN261 |
B | THR262 |
B | GLU263 |
B | ILE264 |
B | ALA301 |
B | PHE337 |
B | ALA338 |
B | ALA346 |
B | SER347 |
B | GLY350 |
B | ASN351 |
B | ILE353 |
B | THR354 |
B | SER359 |
B | ASP360 |
B | LEU404 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FES J 601 |
Chain | Residue |
J | GLN112 |
J | CYS113 |
J | GLY114 |
J | CYS116 |
J | CYS148 |
J | ARG149 |
J | CYS150 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE FES J 602 |
Chain | Residue |
J | GLY42 |
J | CYS43 |
J | GLY44 |
J | GLY46 |
J | GLY47 |
J | CYS48 |
J | GLY49 |
J | CYS51 |
J | CYS73 |
site_id | AC8 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE MTE L 1333 |
Chain | Residue |
J | GLN112 |
J | CYS150 |
L | GLY797 |
L | PHE798 |
L | ARG912 |
L | MET1038 |
L | GLY1039 |
L | GLN1040 |
L | ALA1079 |
L | SER1080 |
L | VAL1081 |
L | SER1082 |
L | GLN1194 |
L | GLU1261 |
L | MOM1334 |
site_id | AC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE MOM L 1334 |
Chain | Residue |
L | PHE911 |
L | ARG912 |
L | ALA1078 |
L | ALA1079 |
L | GLU1261 |
L | MTE1333 |
L | XAN7319 |
L | GLN767 |
L | GLY799 |
L | ALA910 |
site_id | BC1 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE FAD K 606 |
Chain | Residue |
J | GLY46 |
K | LYS256 |
K | LEU257 |
K | VAL258 |
K | VAL259 |
K | GLY260 |
K | ASN261 |
K | THR262 |
K | GLU263 |
K | ILE264 |
K | ALA301 |
K | PHE337 |
K | ALA338 |
K | VAL342 |
K | ALA346 |
K | SER347 |
K | GLY350 |
K | ASN351 |
K | ILE353 |
K | SER359 |
K | ASP360 |
K | LEU404 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FES S 601 |
Chain | Residue |
S | GLN112 |
S | CYS113 |
S | GLY114 |
S | CYS116 |
S | CYS148 |
S | ARG149 |
S | CYS150 |
site_id | BC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE FES S 602 |
Chain | Residue |
S | GLY42 |
S | CYS43 |
S | GLY44 |
S | GLY46 |
S | GLY47 |
S | CYS48 |
S | GLY49 |
S | CYS51 |
S | CYS73 |
site_id | BC4 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE MTE U 1333 |
Chain | Residue |
S | GLN112 |
S | CYS150 |
U | GLY796 |
U | GLY797 |
U | PHE798 |
U | ARG912 |
U | MET1038 |
U | GLY1039 |
U | GLN1040 |
U | ALA1078 |
U | ALA1079 |
U | SER1080 |
U | VAL1081 |
U | SER1082 |
U | GLN1194 |
U | MOM1334 |
site_id | BC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE MOM U 1334 |
Chain | Residue |
U | GLY799 |
U | GLU802 |
U | PHE911 |
U | ARG912 |
U | ALA1078 |
U | ALA1079 |
U | GLU1261 |
U | MTE1333 |
U | XAN7319 |
site_id | BC6 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE FAD T 606 |
Chain | Residue |
S | GLY46 |
T | LYS256 |
T | LEU257 |
T | VAL258 |
T | VAL259 |
T | GLY260 |
T | ASN261 |
T | THR262 |
T | GLU263 |
T | ILE264 |
T | ALA301 |
T | PHE337 |
T | ALA338 |
T | ALA346 |
T | SER347 |
T | GLY350 |
T | ASN351 |
T | ILE353 |
T | THR354 |
T | SER359 |
T | ASP360 |
T | ILE403 |
T | LEU404 |
site_id | BC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FES 2 601 |
Chain | Residue |
2 | GLN112 |
2 | CYS113 |
2 | GLY114 |
2 | CYS116 |
2 | CYS148 |
2 | ARG149 |
2 | CYS150 |
site_id | BC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE FES 2 602 |
Chain | Residue |
2 | GLY42 |
2 | CYS43 |
2 | GLY44 |
2 | GLY46 |
2 | GLY47 |
2 | CYS48 |
2 | GLY49 |
2 | CYS51 |
2 | CYS73 |
site_id | BC9 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE MTE 4 1333 |
Chain | Residue |
2 | GLN112 |
2 | CYS150 |
4 | GLY796 |
4 | GLY797 |
4 | PHE798 |
4 | ARG912 |
4 | MET1038 |
4 | GLY1039 |
4 | GLN1040 |
4 | ALA1078 |
4 | ALA1079 |
4 | SER1080 |
4 | VAL1081 |
4 | SER1082 |
4 | GLN1194 |
4 | MOM1334 |
site_id | CC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE MOM 4 1334 |
Chain | Residue |
4 | GLN767 |
4 | GLY799 |
4 | GLU802 |
4 | PHE911 |
4 | ARG912 |
4 | ALA1078 |
4 | ALA1079 |
4 | GLU1261 |
4 | MTE1333 |
4 | XAN7319 |
site_id | CC2 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE FAD 3 606 |
Chain | Residue |
2 | GLU45 |
2 | GLY46 |
3 | LYS256 |
3 | LEU257 |
3 | VAL258 |
3 | VAL259 |
3 | GLY260 |
3 | ASN261 |
3 | THR262 |
3 | GLU263 |
3 | ILE264 |
3 | ALA301 |
3 | PHE337 |
3 | ALA338 |
3 | ALA346 |
3 | SER347 |
3 | GLY350 |
3 | ASN351 |
3 | ILE353 |
3 | THR354 |
3 | ASP360 |
3 | LEU404 |
site_id | CC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE XAN U 7319 |
Chain | Residue |
U | GLU802 |
U | ARG880 |
U | PHE914 |
U | SER1008 |
U | PHE1009 |
U | THR1010 |
U | LEU1014 |
U | ALA1079 |
U | GLU1261 |
U | MOM1334 |
site_id | CC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE XAN C 7319 |
Chain | Residue |
C | GLU802 |
C | SER876 |
C | ARG880 |
C | PHE914 |
C | SER1008 |
C | PHE1009 |
C | THR1010 |
C | ALA1079 |
C | MOM1334 |
site_id | CC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE XAN L 7319 |
Chain | Residue |
L | GLU802 |
L | ARG880 |
L | PHE914 |
L | PHE1009 |
L | THR1010 |
L | LEU1014 |
L | ALA1079 |
L | MOM1334 |
site_id | CC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE XAN 4 7319 |
Chain | Residue |
4 | GLU802 |
4 | SER876 |
4 | ARG880 |
4 | PHE914 |
4 | PHE1009 |
4 | THR1010 |
4 | LEU1014 |
4 | ALA1079 |
4 | MOM1334 |
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 | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:15148401 |
Chain | Residue | Details |
C | GLU1261 | |
K | ASP360 | |
K | LEU404 | |
K | LYS422 | |
T | LEU257 | |
T | PHE337 | |
T | SER347 | |
T | ASP360 | |
T | LEU404 | |
T | LYS422 | |
3 | LEU257 | |
L | GLU1261 | |
3 | PHE337 | |
3 | SER347 | |
3 | ASP360 | |
3 | LEU404 | |
3 | LYS422 | |
2 | CYS43 | |
2 | CYS48 | |
2 | CYS51 | |
2 | CYS73 | |
2 | CYS113 | |
U | GLU1261 | |
2 | CYS116 | |
2 | CYS148 | |
2 | CYS150 | |
4 | GLU1261 | |
B | LEU404 | |
B | LYS422 | |
K | LEU257 | |
K | PHE337 | |
K | SER347 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252 |
Chain | Residue | Details |
C | GLN767 | |
U | PHE798 | |
U | ARG912 | |
U | ALA1079 | |
4 | GLN767 | |
4 | PHE798 | |
4 | ARG912 | |
4 | ALA1079 | |
C | PHE798 | |
C | ARG912 | |
C | ALA1079 | |
L | GLN767 | |
L | PHE798 | |
L | ARG912 | |
L | ALA1079 | |
U | GLN767 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
C | GLU802 | |
U | ARG880 | |
U | PHE914 | |
U | THR1010 | |
4 | GLU802 | |
4 | ARG880 | |
4 | PHE914 | |
4 | THR1010 | |
C | ARG880 | |
C | PHE914 | |
C | THR1010 | |
L | GLU802 | |
L | ARG880 | |
L | PHE914 | |
L | THR1010 | |
U | GLU802 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1fiq |
Chain | Residue | Details |
C | GLU1261 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1fiq |
Chain | Residue | Details |
L | GLU1261 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1fiq |
Chain | Residue | Details |
U | GLU1261 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1fiq |
Chain | Residue | Details |
4 | GLU1261 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1fiq |
Chain | Residue | Details |
C | ARG912 | |
C | GLN767 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1fiq |
Chain | Residue | Details |
L | ARG912 | |
L | GLN767 |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1fiq |
Chain | Residue | Details |
U | ARG912 | |
U | GLN767 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1fiq |
Chain | Residue | Details |
4 | ARG912 | |
4 | GLN767 |
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 |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 139 |
Chain | Residue | Details |
L | GLU802 | electrostatic stabiliser, hydrogen bond acceptor |
L | ARG880 | electrostatic stabiliser, hydrogen bond donor |
L | GLU1261 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA3 |
Number of Residues | 3 |
Details | M-CSA 139 |
Chain | Residue | Details |
U | GLU802 | electrostatic stabiliser, hydrogen bond acceptor |
U | ARG880 | electrostatic stabiliser, hydrogen bond donor |
U | GLU1261 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA4 |
Number of Residues | 3 |
Details | M-CSA 139 |
Chain | Residue | Details |
4 | GLU802 | electrostatic stabiliser, hydrogen bond acceptor |
4 | ARG880 | electrostatic stabiliser, hydrogen bond donor |
4 | GLU1261 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |