5T5M
TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE FROM METHANOTHERMOBACTER WOLFEII, TRIGONAL FORM AT 2.5 A.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
A | 0046872 | molecular_function | metal ion binding |
B | 0003954 | molecular_function | NADH dehydrogenase activity |
B | 0015948 | biological_process | methanogenesis |
B | 0016020 | cellular_component | membrane |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0018493 | molecular_function | formylmethanofuran dehydrogenase activity |
B | 0022904 | biological_process | respiratory electron transport chain |
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 |
C | 0015948 | biological_process | methanogenesis |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0018493 | molecular_function | formylmethanofuran dehydrogenase activity |
C | 0019386 | biological_process | methanogenesis, from carbon dioxide |
C | 0046914 | molecular_function | transition metal ion binding |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0043546 | molecular_function | molybdopterin cofactor binding |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0046872 | molecular_function | metal ion binding |
F | 0051536 | molecular_function | iron-sulfur cluster binding |
F | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
G | 0016491 | molecular_function | oxidoreductase activity |
G | 0046872 | molecular_function | metal ion binding |
G | 0051536 | molecular_function | iron-sulfur cluster binding |
G | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue MG A 601 |
Chain | Residue |
A | VAL340 |
A | THR344 |
A | HOH729 |
A | HOH738 |
B | GLU138 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue ZN A 602 |
Chain | Residue |
A | HOH720 |
A | KCX178 |
A | HIS231 |
A | HIS271 |
A | ZN603 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue ZN A 603 |
Chain | Residue |
A | HIS57 |
A | HIS59 |
A | KCX178 |
A | ASP385 |
A | ZN602 |
A | HOH720 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue MG A 604 |
Chain | Residue |
A | ARG69 |
A | ARG72 |
A | SER76 |
A | HOH726 |
A | HOH757 |
B | GLY305 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue GOL A 605 |
Chain | Residue |
A | TRP190 |
A | GLY191 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue GOL A 606 |
Chain | Residue |
A | LYS77 |
C | GLU82 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue K B 501 |
Chain | Residue |
B | SER40 |
B | VAL43 |
D | GLU18 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue SF4 B 502 |
Chain | Residue |
B | CYS9 |
B | CYS12 |
B | CYS16 |
B | CYS35 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue W B 503 |
Chain | Residue |
B | CYS118 |
B | MGD504 |
B | MGD505 |
B | H2S506 |
site_id | AD1 |
Number of Residues | 34 |
Details | binding site for residue MGD B 504 |
Chain | Residue |
B | LYS41 |
B | CYS91 |
B | THR114 |
B | VAL117 |
B | CYS118 |
B | MET254 |
B | HIS258 |
B | HIS290 |
B | ALA342 |
B | SER343 |
B | ASP344 |
B | HIS348 |
B | ILE365 |
B | GLU366 |
B | PRO367 |
B | HIS368 |
B | THR370 |
B | PRO382 |
B | ILE384 |
B | VAL385 |
B | ASP414 |
B | W503 |
B | MGD505 |
B | H2S506 |
B | HOH603 |
B | HOH612 |
B | HOH623 |
D | THR7 |
D | ARG9 |
D | LYS21 |
D | MET80 |
D | ASN85 |
D | PHE100 |
D | LYS101 |
site_id | AD2 |
Number of Residues | 37 |
Details | binding site for residue MGD B 505 |
Chain | Residue |
D | GLY8 |
D | ARG9 |
D | THR10 |
D | GLN13 |
D | GLY14 |
D | ILE17 |
D | MET80 |
D | LYS101 |
D | ASN102 |
B | PHE11 |
B | ILE37 |
B | CYS118 |
B | GLY150 |
B | CYS151 |
B | ASN152 |
B | HIS155 |
B | ALA156 |
B | VAL184 |
B | ASP185 |
B | PRO186 |
B | ARG187 |
B | THR189 |
B | PHE203 |
B | ASP204 |
B | ASP206 |
B | GLY253 |
B | MET254 |
B | GLY255 |
B | SER259 |
B | GLY289 |
B | HIS290 |
B | W503 |
B | MGD504 |
B | H2S506 |
B | HOH631 |
B | HOH637 |
D | ASN6 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue H2S B 506 |
Chain | Residue |
B | THR114 |
B | CYS118 |
B | HIS290 |
B | W503 |
B | MGD504 |
B | MGD505 |
site_id | AD4 |
Number of Residues | 7 |
Details | binding site for residue MG C 301 |
Chain | Residue |
B | ASP128 |
B | HOH609 |
B | HOH654 |
C | SER139 |
C | TYR140 |
C | GLY142 |
C | ASP143 |
site_id | AD5 |
Number of Residues | 2 |
Details | binding site for residue GOL D 201 |
Chain | Residue |
D | ARG89 |
D | TYR91 |
site_id | AD6 |
Number of Residues | 6 |
Details | binding site for residue SF4 F 501 |
Chain | Residue |
F | CYS154 |
F | TYR156 |
F | CYS157 |
F | GLY158 |
F | CYS160 |
F | CYS204 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue SF4 F 502 |
Chain | Residue |
F | CYS164 |
F | CYS194 |
F | CYS197 |
F | GLY198 |
F | CYS200 |
site_id | AD8 |
Number of Residues | 4 |
Details | binding site for residue SF4 F 503 |
Chain | Residue |
F | CYS281 |
F | CYS308 |
F | CYS311 |
F | CYS314 |
site_id | AD9 |
Number of Residues | 6 |
Details | binding site for residue SF4 F 504 |
Chain | Residue |
F | CYS271 |
F | CYS274 |
F | GLU275 |
F | CYS277 |
F | CYS318 |
F | ILE323 |
site_id | AE1 |
Number of Residues | 6 |
Details | binding site for residue SF4 F 505 |
Chain | Residue |
F | LEU24 |
F | CYS41 |
F | CYS71 |
F | CYS74 |
F | GLY75 |
F | CYS77 |
site_id | AE2 |
Number of Residues | 6 |
Details | binding site for residue SF4 F 506 |
Chain | Residue |
F | CYS31 |
F | CYS34 |
F | GLY35 |
F | CYS37 |
F | CYS81 |
F | PHE83 |
site_id | AE3 |
Number of Residues | 8 |
Details | binding site for residue SF4 F 507 |
Chain | Residue |
F | CYS125 |
F | ILE130 |
F | CYS239 |
F | VAL240 |
F | ASN241 |
F | CYS242 |
F | GLY243 |
F | CYS245 |
site_id | AE4 |
Number of Residues | 6 |
Details | binding site for residue SF4 F 508 |
Chain | Residue |
F | CYS115 |
F | ILE116 |
F | CYS118 |
F | LYS119 |
F | CYS121 |
F | CYS249 |
site_id | AE5 |
Number of Residues | 6 |
Details | binding site for residue SF4 G 200 |
Chain | Residue |
G | CYS12 |
G | HIS13 |
G | CYS15 |
G | GLY16 |
G | CYS18 |
G | CYS71 |
site_id | AE6 |
Number of Residues | 5 |
Details | binding site for residue SF4 G 201 |
Chain | Residue |
G | CYS22 |
G | CYS61 |
G | CYS64 |
G | GLY65 |
G | CYS67 |
Functional Information from PROSITE/UniProt
site_id | PS00198 |
Number of Residues | 12 |
Details | 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CaVCGlCGeICP |
Chain | Residue | Details |
F | CYS31-PRO42 | |
G | CYS61-PRO72 | |
F | CYS71-PRO82 | |
F | CYS115-PRO126 | |
F | CYS154-PRO165 | |
F | CYS194-PRO205 | |
F | CYS239-PRO250 | |
F | CYS271-PRO282 | |
F | CYS308-PRO319 | |
G | CYS12-PRO23 |