4UEW
Structure of H2-treated anaerobically purified D. fructosovorans NiFe- hydrogenase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008901 | molecular_function | ferredoxin hydrogenase activity |
A | 0009375 | cellular_component | ferredoxin hydrogenase complex |
A | 0051536 | molecular_function | iron-sulfur cluster binding |
B | 0008901 | molecular_function | ferredoxin hydrogenase activity |
B | 0009375 | cellular_component | ferredoxin hydrogenase complex |
B | 0051536 | molecular_function | iron-sulfur cluster binding |
C | 0008901 | molecular_function | ferredoxin hydrogenase activity |
C | 0009375 | cellular_component | ferredoxin hydrogenase complex |
C | 0051536 | molecular_function | iron-sulfur cluster binding |
Q | 0008901 | molecular_function | ferredoxin hydrogenase activity |
Q | 0016151 | molecular_function | nickel cation binding |
Q | 0016491 | molecular_function | oxidoreductase activity |
Q | 0046872 | molecular_function | metal ion binding |
R | 0008901 | molecular_function | ferredoxin hydrogenase activity |
R | 0016151 | molecular_function | nickel cation binding |
R | 0016491 | molecular_function | oxidoreductase activity |
R | 0046872 | molecular_function | metal ion binding |
S | 0008901 | molecular_function | ferredoxin hydrogenase activity |
S | 0016151 | molecular_function | nickel cation binding |
S | 0016491 | molecular_function | oxidoreductase activity |
S | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SF4 A 1265 |
Chain | Residue |
A | HIS184 |
A | CYS187 |
A | ARG189 |
A | LEU190 |
A | CYS212 |
A | LEU213 |
A | CYS218 |
A | PRO221 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE F3S A 1266 |
Chain | Residue |
A | CYS227 |
A | PHE232 |
A | TRP237 |
A | CYS245 |
A | LEU246 |
A | CYS248 |
Q | LYS225 |
Q | GLN230 |
A | ASN225 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SF4 A 1267 |
Chain | Residue |
A | GLU16 |
A | CYS17 |
A | CYS20 |
A | THR113 |
A | CYS114 |
A | GLY146 |
A | CYS147 |
A | PRO148 |
Q | ARG70 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 1271 |
Chain | Residue |
A | ASP168 |
A | LEU169 |
A | LYS176 |
A | GOL1272 |
A | HOH2309 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 1272 |
Chain | Residue |
A | LYS140 |
A | LEU169 |
A | ASP170 |
A | GLU171 |
A | GOL1271 |
A | HOH2204 |
A | HOH2308 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 1273 |
Chain | Residue |
A | ARG6 |
A | LEU37 |
A | HOH2310 |
Q | ALA169 |
Q | PHE170 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SF4 B 1265 |
Chain | Residue |
B | HIS184 |
B | CYS187 |
B | ARG189 |
B | LEU190 |
B | CYS212 |
B | LEU213 |
B | CYS218 |
B | PRO221 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE F3S B 1266 |
Chain | Residue |
B | ASN225 |
B | CYS227 |
B | PHE232 |
B | TRP237 |
B | CYS245 |
B | LEU246 |
B | CYS248 |
R | LYS225 |
R | GLN230 |
site_id | AC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SF4 B 1267 |
Chain | Residue |
B | GLU16 |
B | CYS17 |
B | CYS20 |
B | THR113 |
B | CYS114 |
B | GLY146 |
B | CYS147 |
B | PRO148 |
R | ARG70 |
R | HIS228 |
site_id | BC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SF4 C 1265 |
Chain | Residue |
C | HIS184 |
C | CYS187 |
C | ARG189 |
C | LEU190 |
C | CYS212 |
C | LEU213 |
C | CYS218 |
C | PRO221 |
site_id | BC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE F3S C 1266 |
Chain | Residue |
C | THR223 |
C | ASN225 |
C | CYS227 |
C | PHE232 |
C | TRP237 |
C | CYS245 |
C | LEU246 |
C | CYS248 |
S | LYS225 |
S | GLN230 |
site_id | BC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE SF4 C 1267 |
Chain | Residue |
S | HIS228 |
C | GLU16 |
C | CYS17 |
C | GLY19 |
C | CYS20 |
C | GLY112 |
C | THR113 |
C | CYS114 |
C | GLY146 |
C | CYS147 |
C | PRO148 |
S | ARG70 |
site_id | BC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE FCO Q 1550 |
Chain | Residue |
Q | CYS75 |
Q | VAL78 |
Q | HIS79 |
Q | ALA474 |
Q | PRO475 |
Q | ARG476 |
Q | LEU479 |
Q | VAL497 |
Q | PRO498 |
Q | SER499 |
Q | CSO543 |
Q | CYS546 |
Q | NI1551 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NI Q 1551 |
Chain | Residue |
Q | CYS72 |
Q | CYS75 |
Q | CSO543 |
Q | CYS546 |
Q | FCO1550 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG Q 1553 |
Chain | Residue |
Q | GLU53 |
Q | LEU495 |
Q | HIS549 |
Q | HOH2046 |
Q | HOH2047 |
Q | HOH2283 |
site_id | BC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL Q 1561 |
Chain | Residue |
Q | ARG100 |
Q | ASN104 |
Q | PHE295 |
Q | ALA296 |
Q | THR297 |
Q | GLU445 |
Q | HOH2104 |
Q | HOH2404 |
site_id | BC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL Q 1562 |
Chain | Residue |
A | ALA55 |
C | PHE198 |
C | HOH2157 |
C | HOH2177 |
Q | ASN181 |
Q | ALA182 |
Q | TYR183 |
Q | LEU185 |
Q | ARG529 |
site_id | BC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL Q 1563 |
Chain | Residue |
Q | GLY281 |
Q | GLY282 |
Q | ILE283 |
Q | GLY284 |
Q | GLY285 |
Q | ARG319 |
Q | THR416 |
Q | HIS419 |
Q | HOH2266 |
Q | HOH2341 |
site_id | CC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL Q 1564 |
Chain | Residue |
Q | LYS245 |
Q | LYS337 |
Q | TYR338 |
Q | ASP366 |
Q | HOH2405 |
site_id | CC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE FCO R 1550 |
Chain | Residue |
R | CYS75 |
R | VAL78 |
R | HIS79 |
R | ALA474 |
R | PRO475 |
R | ARG476 |
R | LEU479 |
R | VAL497 |
R | PRO498 |
R | SER499 |
R | CSO543 |
R | CYS546 |
R | NI1551 |
site_id | CC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NI R 1551 |
Chain | Residue |
R | CYS72 |
R | CYS75 |
R | CSO543 |
R | CYS546 |
R | FCO1550 |
site_id | CC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG R 1553 |
Chain | Residue |
R | GLU53 |
R | LEU495 |
R | HIS549 |
R | HOH2049 |
R | HOH2050 |
R | HOH2240 |
site_id | CC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL R 1561 |
Chain | Residue |
B | ALA55 |
R | ASN181 |
R | ALA182 |
R | TYR183 |
R | LEU185 |
R | ARG529 |
R | HOH2340 |
site_id | CC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL R 1562 |
Chain | Residue |
B | LEU137 |
R | LYS410 |
R | HOH2299 |
site_id | CC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL R 1563 |
Chain | Residue |
R | ARG100 |
R | ASN104 |
R | PHE295 |
R | ALA296 |
R | THR297 |
R | GLN310 |
R | GLU445 |
R | HOH2089 |
R | HOH2216 |
site_id | CC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL R 1564 |
Chain | Residue |
R | GLY281 |
R | GLY282 |
R | ILE283 |
R | GLY284 |
R | GLY285 |
R | ARG319 |
R | HIS419 |
R | HOH2194 |
R | HOH2195 |
R | HOH2228 |
site_id | CC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL R 1565 |
Chain | Residue |
R | THR286 |
R | SER287 |
R | ASN288 |
R | ALA380 |
R | PRO514 |
R | HOH2197 |
R | HOH2333 |
site_id | DC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL R 1566 |
Chain | Residue |
R | ARG152 |
R | PRO153 |
R | SER156 |
R | HOH2115 |
R | HOH2121 |
R | HOH2341 |
R | HOH2342 |
S | ALA451 |
site_id | DC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE FCO S 1550 |
Chain | Residue |
S | CYS75 |
S | VAL78 |
S | HIS79 |
S | ALA474 |
S | PRO475 |
S | ARG476 |
S | LEU479 |
S | VAL497 |
S | PRO498 |
S | SER499 |
S | CSO543 |
S | CYS546 |
S | NI1551 |
site_id | DC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NI S 1551 |
Chain | Residue |
S | CYS72 |
S | CYS75 |
S | CSO543 |
S | CYS546 |
S | FCO1550 |
site_id | DC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG S 1553 |
Chain | Residue |
S | GLU53 |
S | LEU495 |
S | HIS549 |
S | HOH2021 |
S | HOH2022 |
S | HOH2166 |
site_id | DC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL S 1561 |
Chain | Residue |
S | ARG100 |
S | ASN104 |
S | PHE295 |
S | ALA296 |
S | THR297 |
S | GLU445 |
S | HOH2153 |
S | HOH2236 |
Functional Information from PROSITE/UniProt
site_id | PS00507 |
Number of Residues | 26 |
Details | NI_HGENASE_L_1 Nickel-dependent hydrogenases large subunit signature 1. RGLEiilkgrdprdaqhftQRaCGVC |
Chain | Residue | Details |
Q | ARG50-CYS75 |
site_id | PS00508 |
Number of Residues | 10 |
Details | NI_HGENASE_L_2 Nickel-dependent hydrogenases large subunit signature 2. FDPCIACgv.H |
Chain | Residue | Details |
Q | PHE540-HIS549 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255 |
Chain | Residue | Details |
S | CYS72 | |
S | CYS75 | |
S | CSO543 | |
S | CYS546 | |
B | CYS20 | |
B | CYS114 | |
B | CYS147 | |
B | HIS184 | |
B | CYS187 | |
B | CYS212 | |
B | CYS218 | |
B | CYS227 | |
B | CYS245 | |
B | CYS248 | |
C | CYS17 | |
C | CYS20 | |
C | CYS114 | |
C | CYS147 | |
C | HIS184 | |
C | CYS187 | |
C | CYS212 | |
C | CYS218 | |
C | CYS227 | |
C | CYS245 | |
C | CYS248 | |
Q | CYS72 | |
Q | CYS75 | |
Q | CSO543 | |
Q | CYS546 | |
R | CYS72 | |
R | CYS75 | |
R | CSO543 | |
R | CYS546 |