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 | 12 |
Details | BINDING: BINDING => ECO:0000255 |
Chain | Residue | Details |
H | CYS72 | |
H | CYS75 | |
H | CYS543 | |
H | CYS546 | |
I | CYS72 | |
I | CYS75 | |
I | CYS543 | |
I | CYS546 | |
J | CYS72 | |
J | CYS75 | |
J | CYS543 | |
J | 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 |