4UQL
High-resolution structure of a Ni-A Ni-Sox mixture of the D. fructosovorans NiFe-hydrogenase L122A mutant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0009061 | biological_process | anaerobic respiration |
| A | 0009375 | cellular_component | ferredoxin hydrogenase complex |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0044569 | cellular_component | [Ni-Fe] hydrogenase complex |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047806 | molecular_function | cytochrome-c3 hydrogenase activity |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0009061 | biological_process | anaerobic respiration |
| B | 0009375 | cellular_component | ferredoxin hydrogenase complex |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0044569 | cellular_component | [Ni-Fe] hydrogenase complex |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047806 | molecular_function | cytochrome-c3 hydrogenase activity |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| Q | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| Q | 0016151 | molecular_function | nickel cation binding |
| Q | 0016491 | molecular_function | oxidoreductase activity |
| Q | 0042597 | cellular_component | periplasmic space |
| Q | 0046872 | molecular_function | metal ion binding |
| Q | 0047806 | molecular_function | cytochrome-c3 hydrogenase activity |
| R | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| R | 0016151 | molecular_function | nickel cation binding |
| R | 0016491 | molecular_function | oxidoreductase activity |
| R | 0042597 | cellular_component | periplasmic space |
| R | 0046872 | molecular_function | metal ion binding |
| R | 0047806 | molecular_function | cytochrome-c3 hydrogenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 A 1265 |
| Chain | Residue |
| A | HIS184 |
| A | CYS187 |
| A | ARG189 |
| A | LEU190 |
| A | CYS212 |
| A | LEU213 |
| A | CYS218 |
| site_id | AC2 |
| Number of Residues | 10 |
| 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 | THR223 |
| 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 | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 1268 |
| Chain | Residue |
| A | ASP82 |
| A | GLN85 |
| A | HOH2060 |
| A | HOH2069 |
| A | HOH2078 |
| B | GLN129 |
| B | LYS131 |
| Q | THR360 |
| Q | HOH2094 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1269 |
| Chain | Residue |
| A | GLN62 |
| A | HOH2048 |
| A | HOH2053 |
| A | HOH2056 |
| A | HOH2141 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GLY B 301 |
| Chain | Residue |
| B | GLY107 |
| B | ILE108 |
| B | LYS140 |
| B | HOH2227 |
| B | HOH2296 |
| B | HOH2306 |
| 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 | 10 |
| Details | BINDING SITE FOR RESIDUE F3S B 1266 |
| Chain | Residue |
| B | THR223 |
| B | ASN225 |
| B | CYS227 |
| B | PHE232 |
| B | TRP237 |
| B | CYS245 |
| B | LEU246 |
| B | CYS248 |
| R | LYS225 |
| R | GLN230 |
| site_id | AC9 |
| Number of Residues | 9 |
| 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 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SOT B 1268 |
| Chain | Residue |
| B | TYR214 |
| B | PRO221 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 1269 |
| Chain | Residue |
| B | GLU205 |
| B | LYS209 |
| B | GOL1272 |
| B | HOH2043 |
| B | HOH2163 |
| B | HOH2255 |
| B | HOH2305 |
| R | ASN454 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 1270 |
| Chain | Residue |
| B | H2S1271 |
| B | HOH2046 |
| B | HOH2075 |
| B | HOH2090 |
| B | HOH2143 |
| B | HOH2155 |
| B | HOH2290 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE H2S B 1271 |
| Chain | Residue |
| B | HIS5 |
| B | ASP68 |
| B | GOL1270 |
| B | HOH2082 |
| B | HOH2090 |
| B | HOH2143 |
| R | GLN175 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GLY Q 601 |
| Chain | Residue |
| Q | HIS118 |
| Q | ASP541 |
| Q | HOH2005 |
| Q | HOH2006 |
| Q | HOH2071 |
| Q | HOH2078 |
| Q | ILE24 |
| Q | GLU25 |
| site_id | BC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE FCO Q 1550 |
| Chain | Residue |
| Q | CSX75 |
| Q | VAL78 |
| Q | HIS79 |
| Q | ALA474 |
| Q | PRO475 |
| Q | ARG476 |
| Q | LEU479 |
| Q | VAL497 |
| Q | PRO498 |
| Q | SER499 |
| Q | CYS546 |
| Q | NI1551 |
| Q | HOH2001 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI Q 1551 |
| Chain | Residue |
| Q | CYS72 |
| Q | CSX75 |
| Q | CSS543 |
| Q | CYS546 |
| Q | FCO1550 |
| Q | HOH2001 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG Q 1552 |
| Chain | Residue |
| Q | GLU53 |
| Q | LEU495 |
| Q | HIS549 |
| Q | HOH2002 |
| Q | HOH2003 |
| Q | HOH2004 |
| site_id | BC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL Q 1553 |
| Chain | Residue |
| Q | ARG100 |
| Q | ASN104 |
| Q | PHE295 |
| Q | ALA296 |
| Q | THR297 |
| Q | GLU445 |
| Q | HOH2007 |
| Q | HOH2095 |
| Q | HOH2120 |
| site_id | CC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL Q 1554 |
| Chain | Residue |
| Q | LYS189 |
| Q | ARG529 |
| site_id | CC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GLY R 601 |
| Chain | Residue |
| R | ILE24 |
| R | GLU25 |
| R | HIS118 |
| R | ARG476 |
| R | ASP541 |
| R | HOH2005 |
| R | HOH2006 |
| R | HOH2007 |
| R | HOH2008 |
| R | HOH2093 |
| site_id | CC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE FCO R 1550 |
| Chain | Residue |
| R | CSX75 |
| R | VAL78 |
| R | HIS79 |
| R | ALA474 |
| R | PRO475 |
| R | ARG476 |
| R | LEU479 |
| R | VAL497 |
| R | PRO498 |
| R | SER499 |
| R | CYS546 |
| R | NI1551 |
| R | HOH2001 |
| site_id | CC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI R 1551 |
| Chain | Residue |
| R | CYS72 |
| R | CSX75 |
| R | CSS543 |
| R | CYS546 |
| R | FCO1550 |
| R | HOH2001 |
| site_id | CC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG R 1552 |
| Chain | Residue |
| R | GLU53 |
| R | LEU495 |
| R | HIS549 |
| R | HOH2002 |
| R | HOH2003 |
| R | HOH2004 |
| site_id | CC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL R 1553 |
| Chain | Residue |
| R | ARG100 |
| R | ASN104 |
| R | PHE295 |
| R | ALA296 |
| R | THR297 |
| R | GLU445 |
| R | GOL1555 |
| R | HOH2083 |
| R | HOH2104 |
| site_id | CC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL R 1554 |
| Chain | Residue |
| R | SER313 |
| R | ASN326 |
| R | LYS395 |
| R | GOL1556 |
| R | HOH2122 |
| R | HOH2284 |
| R | HOH2294 |
| R | HOH2478 |
| site_id | CC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL R 1555 |
| Chain | Residue |
| R | GLN310 |
| R | TRP442 |
| R | GLU445 |
| R | GOL1553 |
| R | HOH2290 |
| R | HOH2342 |
| R | HOH2584 |
| site_id | CC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 1272 |
| Chain | Residue |
| B | GOL1269 |
| R | ASN454 |
| R | HOH2066 |
| R | HOH2114 |
| R | HOH2247 |
| site_id | DC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL R 1556 |
| Chain | Residue |
| B | LYS106 |
| B | HOH2224 |
| R | GLU303 |
| R | LEU306 |
| R | ASN326 |
| R | VAL327 |
| R | GOL1554 |
| R | HOH2076 |
| R | HOH2385 |
| R | HOH2537 |
| site_id | DC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL R 1557 |
| Chain | Residue |
| R | PRO15 |
| R | VAL17 |
| R | GLU33 |
| R | TRP43 |
| R | LYS365 |
| R | HOH2308 |
| R | HOH2555 |
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-CSX75 |
| 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 | 8 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| Q | CYS72 | |
| A | CYS245 | |
| A | CYS248 | |
| B | CYS17 | |
| B | CYS20 | |
| B | CYS114 | |
| B | CYS147 | |
| B | HIS184 | |
| B | CYS187 | |
| B | CYS212 | |
| B | CYS218 | |
| Q | CSX75 | |
| B | CYS227 | |
| B | CYS245 | |
| B | CYS248 | |
| Q | CSS543 | |
| Q | CYS546 | |
| R | CYS72 | |
| R | CSX75 | |
| R | CSS543 | |
| R | CYS546 | |
| A | CYS227 |
