5AA5
Actinobacterial-type NiFe-hydrogenase from Ralstonia eutropha H16 at 2.85 Angstrom resolution
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 | 0030313 | cellular_component | cell envelope |
| A | 0033748 | molecular_function | hydrogenase (acceptor) activity |
| A | 0044569 | cellular_component | [Ni-Fe] hydrogenase complex |
| A | 0046872 | molecular_function | metal ion binding |
| 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 | 0030313 | cellular_component | cell envelope |
| B | 0033748 | molecular_function | hydrogenase (acceptor) activity |
| B | 0044569 | cellular_component | [Ni-Fe] hydrogenase complex |
| B | 0046872 | molecular_function | metal ion binding |
| 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 |
| C | 0016151 | molecular_function | nickel cation binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0009061 | biological_process | anaerobic respiration |
| D | 0009375 | cellular_component | ferredoxin hydrogenase complex |
| D | 0016020 | cellular_component | membrane |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0030313 | cellular_component | cell envelope |
| D | 0033748 | molecular_function | hydrogenase (acceptor) activity |
| D | 0044569 | cellular_component | [Ni-Fe] hydrogenase complex |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051536 | molecular_function | iron-sulfur cluster binding |
| D | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| D | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| E | 0016151 | molecular_function | nickel cation binding |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| F | 0009055 | molecular_function | electron transfer activity |
| F | 0009061 | biological_process | anaerobic respiration |
| F | 0009375 | cellular_component | ferredoxin hydrogenase complex |
| F | 0016020 | cellular_component | membrane |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0030313 | cellular_component | cell envelope |
| F | 0033748 | molecular_function | hydrogenase (acceptor) activity |
| F | 0044569 | cellular_component | [Ni-Fe] hydrogenase complex |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0051536 | molecular_function | iron-sulfur cluster binding |
| F | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| F | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| G | 0016151 | molecular_function | nickel cation binding |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| H | 0009055 | molecular_function | electron transfer activity |
| H | 0009061 | biological_process | anaerobic respiration |
| H | 0009375 | cellular_component | ferredoxin hydrogenase complex |
| H | 0016020 | cellular_component | membrane |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0030313 | cellular_component | cell envelope |
| H | 0033748 | molecular_function | hydrogenase (acceptor) activity |
| H | 0044569 | cellular_component | [Ni-Fe] hydrogenase complex |
| H | 0046872 | molecular_function | metal ion binding |
| H | 0051536 | molecular_function | iron-sulfur cluster binding |
| H | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| H | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| I | 0016151 | molecular_function | nickel cation binding |
| I | 0046872 | molecular_function | metal ion binding |
| K | 0016151 | molecular_function | nickel cation binding |
| K | 0046872 | molecular_function | metal ion binding |
| L | 0016151 | molecular_function | nickel cation binding |
| L | 0046872 | molecular_function | metal ion binding |
| M | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| M | 0009055 | molecular_function | electron transfer activity |
| M | 0009061 | biological_process | anaerobic respiration |
| M | 0009375 | cellular_component | ferredoxin hydrogenase complex |
| M | 0016020 | cellular_component | membrane |
| M | 0016491 | molecular_function | oxidoreductase activity |
| M | 0030313 | cellular_component | cell envelope |
| M | 0033748 | molecular_function | hydrogenase (acceptor) activity |
| M | 0044569 | cellular_component | [Ni-Fe] hydrogenase complex |
| M | 0046872 | molecular_function | metal ion binding |
| M | 0051536 | molecular_function | iron-sulfur cluster binding |
| M | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| M | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 A 501 |
| Chain | Residue |
| A | HIS228 |
| A | CYS231 |
| A | ARG233 |
| A | ALA234 |
| A | CYS251 |
| A | ILE252 |
| A | VAL253 |
| A | CYS257 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 A 502 |
| Chain | Residue |
| A | CYS278 |
| A | CYS285 |
| A | ILE286 |
| A | CYS288 |
| A | THR289 |
| C | ARG203 |
| A | CYS264 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 A 503 |
| Chain | Residue |
| A | GLY31 |
| A | CYS32 |
| A | ASP35 |
| A | THR144 |
| A | CYS145 |
| A | GLY185 |
| A | CYS186 |
| A | PRO187 |
| C | ARG79 |
| C | HIS206 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MLA A 504 |
| Chain | Residue |
| A | TYR237 |
| A | GLY306 |
| A | ALA307 |
| F | ARG325 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MLA A 505 |
| Chain | Residue |
| A | PRO267 |
| A | LYS268 |
| A | GLY274 |
| F | ASP232 |
| F | PRO267 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 B 501 |
| Chain | Residue |
| B | HIS228 |
| B | CYS231 |
| B | ALA234 |
| B | CYS251 |
| B | ILE252 |
| B | VAL253 |
| B | CYS257 |
| B | PRO279 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 B 502 |
| Chain | Residue |
| B | VAL227 |
| B | VAL262 |
| B | CYS264 |
| B | VAL266 |
| B | CYS278 |
| B | CYS285 |
| B | ILE286 |
| B | CYS288 |
| B | THR289 |
| G | ARG203 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 B 503 |
| Chain | Residue |
| B | GLY31 |
| B | CYS32 |
| B | ASP35 |
| B | THR144 |
| B | CYS145 |
| B | GLY185 |
| B | CYS186 |
| B | PRO187 |
| G | ARG79 |
| G | HIS206 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE NFU C 701 |
| Chain | Residue |
| C | CYS81 |
| C | CYS84 |
| C | HIS88 |
| C | ALA499 |
| C | VAL500 |
| C | ARG501 |
| C | LEU504 |
| C | PRO522 |
| C | PRO523 |
| C | THR524 |
| C | CYS573 |
| C | CYS576 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MLA D 701 |
| Chain | Residue |
| B | ARG325 |
| D | TYR237 |
| D | PRO260 |
| D | PRO304 |
| D | GLY306 |
| D | ALA307 |
| D | SER310 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 D 702 |
| Chain | Residue |
| D | HIS228 |
| D | CYS231 |
| D | ARG233 |
| D | ALA234 |
| D | CYS251 |
| D | ILE252 |
| D | VAL253 |
| D | CYS257 |
| D | PRO260 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 D 703 |
| Chain | Residue |
| D | VAL262 |
| D | CYS264 |
| D | VAL266 |
| D | CYS278 |
| D | CYS285 |
| D | ILE286 |
| D | CYS288 |
| D | THR289 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 D 704 |
| Chain | Residue |
| D | ASP35 |
| D | THR144 |
| D | CYS145 |
| D | GLY185 |
| D | CYS186 |
| D | PRO187 |
| E | ARG79 |
| E | HIS206 |
| D | CYS32 |
| site_id | BC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE NFU E 701 |
| Chain | Residue |
| E | CYS81 |
| E | CYS84 |
| E | HIS88 |
| E | ALA499 |
| E | VAL500 |
| E | ARG501 |
| E | LEU504 |
| E | PRO522 |
| E | PRO523 |
| E | THR524 |
| E | CYS573 |
| E | CYS576 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MLA F 701 |
| Chain | Residue |
| A | ARG325 |
| F | TYR237 |
| F | PRO260 |
| F | VAL261 |
| F | ALA307 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 F 702 |
| Chain | Residue |
| F | HIS228 |
| F | CYS231 |
| F | ARG233 |
| F | CYS251 |
| F | ILE252 |
| F | VAL253 |
| F | CYS257 |
| F | PRO279 |
| site_id | BC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 F 703 |
| Chain | Residue |
| F | VAL227 |
| F | CYS264 |
| F | CYS278 |
| F | CYS285 |
| F | ILE286 |
| F | CYS288 |
| F | THR289 |
| L | ARG203 |
| site_id | BC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 F 704 |
| Chain | Residue |
| F | GLY31 |
| F | CYS32 |
| F | ASP35 |
| F | THR144 |
| F | CYS145 |
| F | CYS186 |
| F | PRO187 |
| L | HIS206 |
| site_id | CC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE NFU G 701 |
| Chain | Residue |
| G | CYS81 |
| G | CYS84 |
| G | HIS88 |
| G | ALA499 |
| G | VAL500 |
| G | ARG501 |
| G | LEU504 |
| G | PRO522 |
| G | PRO523 |
| G | THR524 |
| G | CYS573 |
| G | CYS576 |
| site_id | CC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 H 501 |
| Chain | Residue |
| H | HIS228 |
| H | CYS231 |
| H | ARG233 |
| H | ALA234 |
| H | CYS251 |
| H | ILE252 |
| H | VAL253 |
| H | CYS257 |
| H | PRO279 |
| site_id | CC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 H 502 |
| Chain | Residue |
| H | VAL227 |
| H | VAL262 |
| H | CYS264 |
| H | VAL266 |
| H | CYS278 |
| H | CYS285 |
| H | ILE286 |
| H | CYS288 |
| H | THR289 |
| K | ARG203 |
| site_id | CC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 H 503 |
| Chain | Residue |
| H | CYS32 |
| H | ASP35 |
| H | THR144 |
| H | CYS145 |
| H | HIS152 |
| H | GLY185 |
| H | CYS186 |
| H | PRO187 |
| K | ARG79 |
| K | HIS206 |
| site_id | CC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE NFU I 701 |
| Chain | Residue |
| I | CYS81 |
| I | CYS84 |
| I | HIS88 |
| I | ALA499 |
| I | VAL500 |
| I | ARG501 |
| I | LEU504 |
| I | PRO522 |
| I | PRO523 |
| I | THR524 |
| I | CYS573 |
| I | CYS576 |
| site_id | CC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE NFU K 701 |
| Chain | Residue |
| K | CYS81 |
| K | CYS84 |
| K | HIS88 |
| K | ALA499 |
| K | VAL500 |
| K | ARG501 |
| K | LEU504 |
| K | PRO522 |
| K | PRO523 |
| K | THR524 |
| K | CYS573 |
| K | CYS576 |
| site_id | CC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE NFU L 701 |
| Chain | Residue |
| L | CYS81 |
| L | CYS84 |
| L | HIS88 |
| L | ALA499 |
| L | VAL500 |
| L | ARG501 |
| L | LEU504 |
| L | PRO522 |
| L | PRO523 |
| L | THR524 |
| L | CYS573 |
| L | CYS576 |
| site_id | CC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MLA A 701 |
| Chain | Residue |
| H | ARG325 |
| M | TYR237 |
| M | PRO260 |
| M | GLY306 |
| M | ALA307 |
| M | SER310 |
| site_id | CC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 M 702 |
| Chain | Residue |
| M | HIS228 |
| M | CYS231 |
| M | ARG233 |
| M | ALA234 |
| M | CYS251 |
| M | ILE252 |
| M | VAL253 |
| M | CYS257 |
| site_id | DC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 M 703 |
| Chain | Residue |
| M | VAL227 |
| M | VAL262 |
| M | CYS264 |
| M | VAL266 |
| M | CYS278 |
| M | CYS285 |
| M | ILE286 |
| M | CYS288 |
| M | THR289 |
| site_id | DC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 M 704 |
| Chain | Residue |
| I | ARG79 |
| I | HIS206 |
| M | GLY31 |
| M | CYS32 |
| M | ASP35 |
| M | THR144 |
| M | CYS145 |
| M | HIS152 |
| M | GLY185 |
| M | CYS186 |
| M | PRO187 |
| site_id | DC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MLA M 705 |
| Chain | Residue |
| H | TYR237 |
| H | PRO260 |
| H | GLY306 |
| H | SER310 |
| M | ARG325 |
