3CUR
Structure of a double methionine mutant 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 | 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 |
| 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 |
| 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 | 0016151 | molecular_function | nickel cation binding |
| I | 0016491 | molecular_function | oxidoreductase activity |
| I | 0042597 | cellular_component | periplasmic space |
| I | 0046872 | molecular_function | metal ion binding |
| I | 0047806 | molecular_function | cytochrome-c3 hydrogenase activity |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NI H 551 |
| Chain | Residue |
| H | CYS72 |
| H | CYS75 |
| H | CYS543 |
| H | CYS546 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG H 553 |
| Chain | Residue |
| H | HOH566 |
| H | GLU53 |
| H | LEU495 |
| H | HIS549 |
| H | HOH564 |
| H | HOH565 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NI I 551 |
| Chain | Residue |
| I | CYS72 |
| I | CYS75 |
| I | CYS543 |
| I | CYS546 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG I 553 |
| Chain | Residue |
| I | GLU53 |
| I | LEU495 |
| I | HIS549 |
| I | HOH565 |
| I | HOH566 |
| I | HOH567 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NI J 551 |
| Chain | Residue |
| J | CYS72 |
| J | CYS75 |
| J | CYS543 |
| J | CYS546 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG J 553 |
| Chain | Residue |
| J | GLU53 |
| J | LEU495 |
| J | HIS549 |
| J | HOH567 |
| J | HOH568 |
| J | HOH569 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 A 265 |
| Chain | Residue |
| A | HIS184 |
| A | CYS187 |
| A | ARG189 |
| A | LEU190 |
| A | CYS212 |
| A | LEU213 |
| A | CYS218 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE F3S A 266 |
| Chain | Residue |
| A | ASN225 |
| A | CYS227 |
| A | PHE232 |
| A | TRP237 |
| A | CYS245 |
| A | LEU246 |
| A | CYS248 |
| H | LYS225 |
| H | GLN230 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 A 267 |
| Chain | Residue |
| A | GLU16 |
| A | CYS17 |
| A | CYS20 |
| A | THR113 |
| A | CYS114 |
| A | GLY146 |
| A | CYS147 |
| A | PRO148 |
| H | ARG70 |
| H | HIS228 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FCO H 550 |
| Chain | Residue |
| H | CYS75 |
| H | HIS79 |
| H | ALA474 |
| H | PRO475 |
| H | ARG476 |
| H | LEU479 |
| H | PRO498 |
| H | SER499 |
| H | CYS546 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PER H 552 |
| Chain | Residue |
| H | CYS75 |
| H | ARG476 |
| H | CYS543 |
| H | CYS546 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 B 265 |
| Chain | Residue |
| B | HIS184 |
| B | CYS187 |
| B | ARG189 |
| B | LEU190 |
| B | CYS212 |
| B | LEU213 |
| B | CYS218 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE F3S B 266 |
| Chain | Residue |
| B | ASN225 |
| B | CYS227 |
| B | PHE232 |
| B | PRO238 |
| B | CYS245 |
| B | LEU246 |
| B | CYS248 |
| I | LYS225 |
| I | GLN230 |
| site_id | BC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 B 267 |
| Chain | Residue |
| B | GLU16 |
| B | CYS17 |
| B | CYS20 |
| B | THR113 |
| B | CYS114 |
| B | GLY146 |
| B | CYS147 |
| B | PRO148 |
| I | ARG70 |
| I | HIS228 |
| site_id | BC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FCO I 550 |
| Chain | Residue |
| I | ARG476 |
| I | LEU479 |
| I | PRO498 |
| I | SER499 |
| I | CYS546 |
| I | CYS75 |
| I | HIS79 |
| I | ALA474 |
| I | PRO475 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PER I 552 |
| Chain | Residue |
| I | CYS75 |
| I | ARG476 |
| I | CYS543 |
| I | CYS546 |
| site_id | BC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 C 265 |
| Chain | Residue |
| C | HIS184 |
| C | CYS187 |
| C | ARG189 |
| C | LEU190 |
| C | CYS212 |
| C | LEU213 |
| C | CYS218 |
| C | PRO221 |
| site_id | BC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE F3S C 266 |
| Chain | Residue |
| C | THR223 |
| C | ASN225 |
| C | CYS227 |
| C | PHE232 |
| C | TRP237 |
| C | CYS245 |
| C | LEU246 |
| C | CYS248 |
| J | GLN230 |
| site_id | CC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 C 267 |
| Chain | Residue |
| C | GLU16 |
| C | CYS17 |
| C | CYS20 |
| C | THR113 |
| C | CYS114 |
| C | GLY146 |
| C | CYS147 |
| C | PRO148 |
| J | ARG70 |
| J | HIS228 |
| site_id | CC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FCO J 550 |
| Chain | Residue |
| J | CYS75 |
| J | HIS79 |
| J | ALA474 |
| J | PRO475 |
| J | ARG476 |
| J | LEU479 |
| J | PRO498 |
| J | SER499 |
| J | CYS546 |
| site_id | CC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PER J 552 |
| Chain | Residue |
| J | CYS75 |
| J | ARG476 |
| J | CYS543 |
| J | CYS546 |
| site_id | CC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL H 561 |
| Chain | Residue |
| H | ARG100 |
| H | ASN104 |
| H | PHE295 |
| H | ALA296 |
| H | THR297 |
| H | GLU445 |
| H | HOH582 |
| H | HOH663 |
| site_id | CC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL H 562 |
| Chain | Residue |
| A | ALA55 |
| C | HOH270 |
| H | ASN181 |
| H | ALA182 |
| H | TYR183 |
| H | LEU185 |
| H | ARG529 |
| H | HOH640 |
| site_id | CC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL I 561 |
| Chain | Residue |
| B | ALA55 |
| I | ASN181 |
| I | ALA182 |
| I | LEU185 |
| I | ARG529 |
| I | HOH570 |
| I | HOH636 |
| site_id | CC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL I 563 |
| Chain | Residue |
| I | ARG100 |
| I | ASN104 |
| I | PHE295 |
| I | ALA296 |
| I | THR297 |
| I | GLU445 |
| I | HOH584 |
| site_id | CC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL I 564 |
| Chain | Residue |
| B | PHE202 |
| B | TYR261 |
| I | ARG62 |
| I | TRP460 |
| I | HOH618 |
| I | HOH635 |
| I | HOH705 |
| site_id | CC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL J 564 |
| Chain | Residue |
| J | GLY450 |
| J | LYS452 |
| J | ASP453 |
| J | ASN454 |
| J | HOH714 |
| site_id | DC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL J 565 |
| Chain | Residue |
| J | ARG100 |
| J | ASN104 |
| J | PHE295 |
| J | ALA296 |
| J | THR297 |
| J | TRP442 |
| J | GLU445 |
| J | HOH582 |
| J | HOH630 |
| J | HOH653 |
Functional Information from PROSITE/UniProt
| site_id | PS00507 |
| Number of Residues | 26 |
| Details | NI_HGENASE_L_1 Nickel-dependent hydrogenases large subunit signature 1. RGLEiilkgrdprdaqhftQRaCGMC |
| Chain | Residue | Details |
| H | 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 |
| H | PHE540-HIS549 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 33 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cc1 |
| Chain | Residue | Details |
| H | GLU25 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cc1 |
| Chain | Residue | Details |
| I | GLU25 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cc1 |
| Chain | Residue | Details |
| J | GLU25 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cc1 |
| Chain | Residue | Details |
| A | THR18 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cc1 |
| Chain | Residue | Details |
| B | THR18 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cc1 |
| Chain | Residue | Details |
| C | THR18 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cc1 |
| Chain | Residue | Details |
| H | CYS543 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cc1 |
| Chain | Residue | Details |
| I | CYS543 |
| site_id | CSA9 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cc1 |
| Chain | Residue | Details |
| J | CYS543 |
