1TV7
Structure of the S-adenosylmethionine dependent Enzyme MoaA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0005525 | molecular_function | GTP binding |
A | 0006777 | biological_process | Mo-molybdopterin cofactor biosynthetic process |
A | 0016829 | molecular_function | lyase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0051536 | molecular_function | iron-sulfur cluster binding |
A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
A | 0061798 | molecular_function | GTP 3',8'-cyclase activity |
A | 0061799 | molecular_function | cyclic pyranopterin monophosphate synthase activity |
A | 1904047 | molecular_function | S-adenosyl-L-methionine binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0005525 | molecular_function | GTP binding |
B | 0006777 | biological_process | Mo-molybdopterin cofactor biosynthetic process |
B | 0016829 | molecular_function | lyase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0051536 | molecular_function | iron-sulfur cluster binding |
B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
B | 0061798 | molecular_function | GTP 3',8'-cyclase activity |
B | 0061799 | molecular_function | cyclic pyranopterin monophosphate synthase activity |
B | 1904047 | molecular_function | S-adenosyl-L-methionine binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 A 1403 |
Chain | Residue |
A | PHE26 |
A | HOH1419 |
A | CYS28 |
A | TYR30 |
A | SER126 |
A | LEU127 |
A | ASP128 |
A | PHE135 |
A | SF41401 |
A | HOH1404 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 2403 |
Chain | Residue |
B | SER126 |
B | LEU127 |
B | ASP128 |
B | PHE135 |
B | ASN165 |
B | HOH2404 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SF4 A 1401 |
Chain | Residue |
A | CYS24 |
A | PHE26 |
A | CYS28 |
A | CYS31 |
A | MET32 |
A | GLY75 |
A | SO41403 |
A | HOH1420 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SF4 A 1402 |
Chain | Residue |
A | CYS261 |
A | CYS264 |
A | CYS278 |
A | LEU279 |
A | ASP314 |
A | SER317 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SF4 B 2401 |
Chain | Residue |
B | CYS24 |
B | PHE26 |
B | CYS28 |
B | CYS31 |
B | MET32 |
B | GLY75 |
B | ASN104 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SF4 B 2402 |
Chain | Residue |
B | ARG11 |
B | CYS261 |
B | CYS264 |
B | CYS278 |
B | LEU279 |
B | ARG312 |
B | SER317 |
Functional Information from PROSITE/UniProt
site_id | PS01305 |
Number of Residues | 12 |
Details | MOAA_NIFB_PQQE moaA / nifB / pqqE family signature. VtdrCNFRCdYC |
Chain | Residue | Details |
A | VAL20-CYS31 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 30 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16632608, ECO:0007744|PDB:2FB3 |
Chain | Residue | Details |
A | ARG17 | |
A | LYS163 | |
A | MET197 | |
A | CYS261 | |
A | CYS264 | |
A | ARG266 | |
A | CYS278 | |
B | ARG17 | |
B | CYS24 | |
B | CYS28 | |
B | TYR30 | |
A | CYS24 | |
B | CYS31 | |
B | ARG71 | |
B | GLY75 | |
B | THR102 | |
B | SER126 | |
B | LYS163 | |
B | MET197 | |
B | CYS261 | |
B | CYS264 | |
B | ARG266 | |
A | CYS28 | |
B | CYS278 | |
A | TYR30 | |
A | CYS31 | |
A | ARG71 | |
A | GLY75 | |
A | THR102 | |
A | SER126 |