2FRV
CRYSTAL STRUCTURE OF THE OXIDIZED FORM OF NI-FE HYDROGENASE
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 | 0016151 | molecular_function | nickel cation binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047806 | molecular_function | cytochrome-c3 hydrogenase activity |
| C | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0009061 | biological_process | anaerobic respiration |
| C | 0009375 | cellular_component | ferredoxin hydrogenase complex |
| C | 0016020 | cellular_component | membrane |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0044569 | cellular_component | [Ni-Fe] hydrogenase complex |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0047806 | molecular_function | cytochrome-c3 hydrogenase activity |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| C | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| D | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| D | 0016151 | molecular_function | nickel cation binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0042597 | cellular_component | periplasmic space |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0047806 | molecular_function | cytochrome-c3 hydrogenase activity |
| E | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| E | 0009055 | molecular_function | electron transfer activity |
| E | 0009061 | biological_process | anaerobic respiration |
| E | 0009375 | cellular_component | ferredoxin hydrogenase complex |
| E | 0016020 | cellular_component | membrane |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0042597 | cellular_component | periplasmic space |
| E | 0044569 | cellular_component | [Ni-Fe] hydrogenase complex |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0047806 | molecular_function | cytochrome-c3 hydrogenase activity |
| E | 0051536 | molecular_function | iron-sulfur cluster binding |
| E | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| E | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| F | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| F | 0016151 | molecular_function | nickel cation binding |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0042597 | cellular_component | periplasmic space |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0047806 | molecular_function | cytochrome-c3 hydrogenase activity |
| G | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| G | 0009055 | molecular_function | electron transfer activity |
| G | 0009061 | biological_process | anaerobic respiration |
| G | 0009375 | cellular_component | ferredoxin hydrogenase complex |
| G | 0016020 | cellular_component | membrane |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0042597 | cellular_component | periplasmic space |
| G | 0044569 | cellular_component | [Ni-Fe] hydrogenase complex |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0047806 | molecular_function | cytochrome-c3 hydrogenase activity |
| G | 0051536 | molecular_function | iron-sulfur cluster binding |
| G | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| G | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| H | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| H | 0016151 | molecular_function | nickel cation binding |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0042597 | cellular_component | periplasmic space |
| H | 0046872 | molecular_function | metal ion binding |
| H | 0047806 | molecular_function | cytochrome-c3 hydrogenase activity |
| I | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| I | 0009055 | molecular_function | electron transfer activity |
| I | 0009061 | biological_process | anaerobic respiration |
| I | 0009375 | cellular_component | ferredoxin hydrogenase complex |
| I | 0016020 | cellular_component | membrane |
| I | 0016491 | molecular_function | oxidoreductase activity |
| I | 0042597 | cellular_component | periplasmic space |
| I | 0044569 | cellular_component | [Ni-Fe] hydrogenase complex |
| I | 0046872 | molecular_function | metal ion binding |
| I | 0047806 | molecular_function | cytochrome-c3 hydrogenase activity |
| I | 0051536 | molecular_function | iron-sulfur cluster binding |
| I | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| I | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| J | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| J | 0016151 | molecular_function | nickel cation binding |
| J | 0016491 | molecular_function | oxidoreductase activity |
| J | 0042597 | cellular_component | periplasmic space |
| J | 0046872 | molecular_function | metal ion binding |
| J | 0047806 | molecular_function | cytochrome-c3 hydrogenase activity |
| L | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| L | 0016151 | molecular_function | nickel cation binding |
| L | 0016491 | molecular_function | oxidoreductase activity |
| L | 0042597 | cellular_component | periplasmic space |
| L | 0046872 | molecular_function | metal ion binding |
| L | 0047806 | molecular_function | cytochrome-c3 hydrogenase activity |
| S | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| S | 0009055 | molecular_function | electron transfer activity |
| S | 0009061 | biological_process | anaerobic respiration |
| S | 0009375 | cellular_component | ferredoxin hydrogenase complex |
| S | 0016020 | cellular_component | membrane |
| S | 0016491 | molecular_function | oxidoreductase activity |
| S | 0042597 | cellular_component | periplasmic space |
| S | 0044569 | cellular_component | [Ni-Fe] hydrogenase complex |
| S | 0046872 | molecular_function | metal ion binding |
| S | 0047806 | molecular_function | cytochrome-c3 hydrogenase activity |
| S | 0051536 | molecular_function | iron-sulfur cluster binding |
| S | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| S | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI L 538 |
| Chain | Residue |
| L | CYS530 |
| L | CYS533 |
| L | FCO537 |
| L | O539 |
| L | CYS65 |
| L | CYS68 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI B 538 |
| Chain | Residue |
| B | CYS65 |
| B | CYS68 |
| B | CYS530 |
| B | CYS533 |
| B | FCO537 |
| B | O539 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI D 538 |
| Chain | Residue |
| D | CYS65 |
| D | CYS68 |
| D | CYS530 |
| D | CYS533 |
| D | FCO537 |
| D | O539 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI F 538 |
| Chain | Residue |
| F | CYS65 |
| F | CYS68 |
| F | CYS530 |
| F | CYS533 |
| F | FCO537 |
| F | O539 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI H 538 |
| Chain | Residue |
| H | CYS65 |
| H | CYS68 |
| H | CYS530 |
| H | CYS533 |
| H | FCO537 |
| H | O539 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI J 538 |
| Chain | Residue |
| J | CYS65 |
| J | CYS68 |
| J | CYS530 |
| J | CYS533 |
| J | FCO537 |
| J | O539 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG L 540 |
| Chain | Residue |
| L | GLU46 |
| L | LEU482 |
| L | HIS536 |
| L | HOH5011 |
| L | HOH5012 |
| L | HOH5013 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 540 |
| Chain | Residue |
| B | GLU46 |
| B | LEU482 |
| B | HIS536 |
| B | HOH5024 |
| B | HOH5025 |
| B | HOH5026 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 540 |
| Chain | Residue |
| D | GLU46 |
| D | LEU482 |
| D | HIS536 |
| D | HOH5037 |
| D | HOH5038 |
| D | HOH5039 |
| site_id | ACT |
| Number of Residues | 7 |
| Details | NI-FE ACTIVE SITE. |
| Chain | Residue |
| L | CYS65 |
| L | CYS68 |
| L | CYS530 |
| L | CYS533 |
| L | FCO537 |
| L | NI538 |
| L | O539 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG F 540 |
| Chain | Residue |
| F | GLU46 |
| F | LEU482 |
| F | HIS536 |
| F | HOH5050 |
| F | HOH5051 |
| F | HOH5052 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG H 540 |
| Chain | Residue |
| H | GLU46 |
| H | LEU482 |
| H | HIS536 |
| H | HOH5063 |
| H | HOH5064 |
| H | HOH5065 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG J 540 |
| Chain | Residue |
| J | GLU46 |
| J | LEU482 |
| J | HIS536 |
| J | HOH5076 |
| J | HOH5077 |
| J | HOH5078 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SF4 S 265 |
| Chain | Residue |
| S | HIS185 |
| S | CYS188 |
| S | CYS213 |
| S | LEU214 |
| S | CYS219 |
| site_id | BC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE F3S S 266 |
| Chain | Residue |
| L | LYS216 |
| L | GLN221 |
| S | THR224 |
| S | ASN226 |
| S | CYS228 |
| S | PHE233 |
| S | TRP238 |
| S | PRO239 |
| S | CYS246 |
| S | ILE247 |
| S | CYS249 |
| site_id | BC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 S 267 |
| Chain | Residue |
| S | CYS20 |
| S | GLY110 |
| S | THR111 |
| S | CYS112 |
| S | GLY147 |
| S | CYS148 |
| S | PRO149 |
| L | ARG63 |
| L | HIS219 |
| S | GLU16 |
| S | CYS17 |
| site_id | BC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE FCO L 537 |
| Chain | Residue |
| L | CYS68 |
| L | VAL71 |
| L | HIS72 |
| L | ALA461 |
| L | PRO462 |
| L | ARG463 |
| L | LEU466 |
| L | VAL484 |
| L | PRO485 |
| L | SER486 |
| L | CYS533 |
| L | NI538 |
| L | O539 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE O L 539 |
| Chain | Residue |
| L | CYS68 |
| L | ARG463 |
| L | CYS530 |
| L | CYS533 |
| L | FCO537 |
| L | NI538 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SF4 A 265 |
| Chain | Residue |
| A | HIS185 |
| A | CYS188 |
| A | CYS213 |
| A | LEU214 |
| A | CYS219 |
| site_id | CC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE F3S A 266 |
| Chain | Residue |
| A | THR224 |
| A | ASN226 |
| A | CYS228 |
| A | PHE233 |
| A | TRP238 |
| A | PRO239 |
| A | CYS246 |
| A | ILE247 |
| A | CYS249 |
| B | LYS216 |
| B | GLN221 |
| site_id | CC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 A 267 |
| Chain | Residue |
| A | GLU16 |
| A | CYS17 |
| A | CYS20 |
| A | GLY110 |
| A | THR111 |
| A | CYS112 |
| A | GLY147 |
| A | CYS148 |
| A | PRO149 |
| B | ARG63 |
| B | HIS219 |
| site_id | CC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE FCO B 537 |
| Chain | Residue |
| B | CYS68 |
| B | VAL71 |
| B | HIS72 |
| B | ALA461 |
| B | PRO462 |
| B | ARG463 |
| B | LEU466 |
| B | VAL484 |
| B | PRO485 |
| B | SER486 |
| B | CYS533 |
| B | NI538 |
| B | O539 |
| site_id | CC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE O B 539 |
| Chain | Residue |
| B | CYS68 |
| B | ARG463 |
| B | CYS530 |
| B | CYS533 |
| B | FCO537 |
| B | NI538 |
| site_id | CC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SF4 C 265 |
| Chain | Residue |
| C | HIS185 |
| C | CYS188 |
| C | CYS213 |
| C | LEU214 |
| C | CYS219 |
| site_id | CC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE F3S C 266 |
| Chain | Residue |
| C | THR224 |
| C | ASN226 |
| C | CYS228 |
| C | PHE233 |
| C | TRP238 |
| C | PRO239 |
| C | CYS246 |
| C | ILE247 |
| C | CYS249 |
| D | LYS216 |
| D | GLN221 |
| site_id | CC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 C 267 |
| Chain | Residue |
| C | GLU16 |
| C | CYS17 |
| C | CYS20 |
| C | GLY110 |
| C | THR111 |
| C | CYS112 |
| C | GLY147 |
| C | CYS148 |
| C | PRO149 |
| D | ARG63 |
| D | HIS219 |
| site_id | CC8 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE FCO D 537 |
| Chain | Residue |
| D | CYS68 |
| D | VAL71 |
| D | HIS72 |
| D | ALA461 |
| D | PRO462 |
| D | ARG463 |
| D | LEU466 |
| D | VAL484 |
| D | PRO485 |
| D | SER486 |
| D | CYS533 |
| D | NI538 |
| D | O539 |
| site_id | CC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE O D 539 |
| Chain | Residue |
| D | CYS68 |
| D | ARG463 |
| D | CYS530 |
| D | CYS533 |
| D | FCO537 |
| D | NI538 |
| site_id | DC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SF4 E 265 |
| Chain | Residue |
| E | HIS185 |
| E | CYS188 |
| E | CYS213 |
| E | LEU214 |
| E | CYS219 |
| site_id | DC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE F3S E 266 |
| Chain | Residue |
| E | THR224 |
| E | ASN226 |
| E | CYS228 |
| E | PHE233 |
| E | TRP238 |
| E | PRO239 |
| E | CYS246 |
| E | ILE247 |
| E | CYS249 |
| F | LYS216 |
| F | GLN221 |
| site_id | DC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 E 267 |
| Chain | Residue |
| E | GLU16 |
| E | CYS17 |
| E | CYS20 |
| E | GLY110 |
| E | THR111 |
| E | CYS112 |
| E | GLY147 |
| E | CYS148 |
| E | PRO149 |
| F | ARG63 |
| F | HIS219 |
| site_id | DC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE FCO F 537 |
| Chain | Residue |
| F | CYS68 |
| F | VAL71 |
| F | HIS72 |
| F | ALA461 |
| F | PRO462 |
| F | ARG463 |
| F | LEU466 |
| F | VAL484 |
| F | PRO485 |
| F | SER486 |
| F | CYS533 |
| F | NI538 |
| F | O539 |
| site_id | DC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE O F 539 |
| Chain | Residue |
| F | CYS68 |
| F | ARG463 |
| F | CYS530 |
| F | CYS533 |
| F | FCO537 |
| F | NI538 |
| site_id | DC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SF4 G 265 |
| Chain | Residue |
| G | HIS185 |
| G | CYS188 |
| G | CYS213 |
| G | LEU214 |
| G | CYS219 |
| site_id | DC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE F3S G 266 |
| Chain | Residue |
| G | THR224 |
| G | ASN226 |
| G | CYS228 |
| G | PHE233 |
| G | TRP238 |
| G | PRO239 |
| G | CYS246 |
| G | ILE247 |
| G | CYS249 |
| H | LYS216 |
| H | GLN221 |
| site_id | DC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 G 267 |
| Chain | Residue |
| G | GLU16 |
| G | CYS17 |
| G | CYS20 |
| G | GLY110 |
| G | THR111 |
| G | CYS112 |
| G | GLY147 |
| G | CYS148 |
| G | PRO149 |
| H | ARG63 |
| H | HIS219 |
| site_id | DC9 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE FCO H 537 |
| Chain | Residue |
| H | CYS68 |
| H | VAL71 |
| H | HIS72 |
| H | ALA461 |
| H | PRO462 |
| H | ARG463 |
| H | LEU466 |
| H | VAL484 |
| H | PRO485 |
| H | SER486 |
| H | CYS533 |
| H | NI538 |
| H | O539 |
| site_id | EC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE O H 539 |
| Chain | Residue |
| H | CYS68 |
| H | ARG463 |
| H | CYS530 |
| H | CYS533 |
| H | FCO537 |
| H | NI538 |
| site_id | EC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SF4 I 265 |
| Chain | Residue |
| I | HIS185 |
| I | CYS188 |
| I | CYS213 |
| I | LEU214 |
| I | CYS219 |
| site_id | EC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE F3S I 266 |
| Chain | Residue |
| I | THR224 |
| I | ASN226 |
| I | CYS228 |
| I | PHE233 |
| I | TRP238 |
| I | PRO239 |
| I | CYS246 |
| I | ILE247 |
| I | CYS249 |
| J | LYS216 |
| J | GLN221 |
| site_id | EC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 I 267 |
| Chain | Residue |
| I | GLU16 |
| I | CYS17 |
| I | CYS20 |
| I | GLY110 |
| I | THR111 |
| I | CYS112 |
| I | GLY147 |
| I | CYS148 |
| I | PRO149 |
| J | ARG63 |
| J | HIS219 |
| site_id | EC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE FCO J 537 |
| Chain | Residue |
| J | CYS68 |
| J | VAL71 |
| J | HIS72 |
| J | ALA461 |
| J | PRO462 |
| J | ARG463 |
| J | LEU466 |
| J | VAL484 |
| J | PRO485 |
| J | SER486 |
| J | CYS533 |
| J | NI538 |
| J | O539 |
| site_id | EC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE O J 539 |
| Chain | Residue |
| J | CYS68 |
| J | ARG463 |
| J | CYS530 |
| J | CYS533 |
| J | FCO537 |
| J | NI538 |
Functional Information from PROSITE/UniProt
| site_id | PS00507 |
| Number of Residues | 26 |
| Details | NI_HGENASE_L_1 Nickel-dependent hydrogenases large subunit signature 1. RGLEmilkgrdprdaqhftQRaCGVC |
| Chain | Residue | Details |
| L | ARG43-CYS68 |
| site_id | PS00508 |
| Number of Residues | 10 |
| Details | NI_HGENASE_L_2 Nickel-dependent hydrogenases large subunit signature 2. YDPCIACgv.H |
| Chain | Residue | Details |
| L | TYR527-HIS536 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 78 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7854413","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cc1 |
| Chain | Residue | Details |
| S | THR18 | |
| L | CYS530 | |
| L | GLU18 |
| site_id | CSA10 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cc1 |
| Chain | Residue | Details |
| F | CYS530 |
| site_id | CSA11 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cc1 |
| Chain | Residue | Details |
| H | CYS530 |
| site_id | CSA12 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cc1 |
| Chain | Residue | Details |
| J | CYS530 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cc1 |
| Chain | Residue | Details |
| A | THR18 | |
| B | CYS530 | |
| B | GLU18 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cc1 |
| Chain | Residue | Details |
| C | THR18 | |
| D | CYS530 | |
| D | GLU18 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cc1 |
| Chain | Residue | Details |
| F | CYS530 | |
| F | GLU18 | |
| E | THR18 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cc1 |
| Chain | Residue | Details |
| H | CYS530 | |
| H | GLU18 | |
| G | THR18 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cc1 |
| Chain | Residue | Details |
| J | CYS530 | |
| J | GLU18 | |
| I | THR18 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cc1 |
| Chain | Residue | Details |
| L | CYS530 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cc1 |
| Chain | Residue | Details |
| B | CYS530 |
| site_id | CSA9 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cc1 |
| Chain | Residue | Details |
| D | CYS530 |
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 126 |
| Chain | Residue | Details |
| B | GLU18 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | CYS65 | activator, metal ligand |
| B | CYS68 | activator, electrostatic stabiliser, metal ligand |
| B | HIS72 | electrostatic stabiliser, hydrogen bond donor |
| B | ARG463 | electrostatic stabiliser, hydrogen bond donor |
| B | SER486 | electrostatic stabiliser, hydrogen bond donor |
| B | CYS530 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| B | CYS533 | activator, electrostatic stabiliser, metal ligand |
| site_id | MCSA2 |
| Number of Residues | 8 |
| Details | M-CSA 126 |
| Chain | Residue | Details |
| D | GLU18 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| D | CYS65 | activator, metal ligand |
| D | CYS68 | activator, electrostatic stabiliser, metal ligand |
| D | HIS72 | electrostatic stabiliser, hydrogen bond donor |
| D | ARG463 | electrostatic stabiliser, hydrogen bond donor |
| D | SER486 | electrostatic stabiliser, hydrogen bond donor |
| D | CYS530 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| D | CYS533 | activator, electrostatic stabiliser, metal ligand |
| site_id | MCSA3 |
| Number of Residues | 8 |
| Details | M-CSA 126 |
| Chain | Residue | Details |
| F | GLU18 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| F | CYS65 | activator, metal ligand |
| F | CYS68 | activator, electrostatic stabiliser, metal ligand |
| F | HIS72 | electrostatic stabiliser, hydrogen bond donor |
| F | ARG463 | electrostatic stabiliser, hydrogen bond donor |
| F | SER486 | electrostatic stabiliser, hydrogen bond donor |
| F | CYS530 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| F | CYS533 | activator, electrostatic stabiliser, metal ligand |
| site_id | MCSA4 |
| Number of Residues | 8 |
| Details | M-CSA 126 |
| Chain | Residue | Details |
| H | GLU18 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| H | CYS65 | activator, metal ligand |
| H | CYS68 | activator, electrostatic stabiliser, metal ligand |
| H | HIS72 | electrostatic stabiliser, hydrogen bond donor |
| H | ARG463 | electrostatic stabiliser, hydrogen bond donor |
| H | SER486 | electrostatic stabiliser, hydrogen bond donor |
| H | CYS530 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| H | CYS533 | activator, electrostatic stabiliser, metal ligand |
| site_id | MCSA5 |
| Number of Residues | 8 |
| Details | M-CSA 126 |
| Chain | Residue | Details |
| J | GLU18 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| J | CYS65 | activator, metal ligand |
| J | CYS68 | activator, electrostatic stabiliser, metal ligand |
| J | HIS72 | electrostatic stabiliser, hydrogen bond donor |
| J | ARG463 | electrostatic stabiliser, hydrogen bond donor |
| J | SER486 | electrostatic stabiliser, hydrogen bond donor |
| J | CYS530 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| J | CYS533 | activator, electrostatic stabiliser, metal ligand |
| site_id | MCSA6 |
| Number of Residues | 8 |
| Details | M-CSA 126 |
| Chain | Residue | Details |
| L | GLU18 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| L | CYS65 | activator, metal ligand |
| L | CYS68 | activator, electrostatic stabiliser, metal ligand |
| L | HIS72 | electrostatic stabiliser, hydrogen bond donor |
| L | ARG463 | electrostatic stabiliser, hydrogen bond donor |
| L | SER486 | electrostatic stabiliser, hydrogen bond donor |
| L | CYS530 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| L | CYS533 | activator, electrostatic stabiliser, metal ligand |
