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 | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:7854413 |
Chain | Residue | Details |
L | GLY66 | |
H | ILE531 | |
J | GLY66 | |
J | ILE531 | |
A | CYS20 | |
A | CYS112 | |
A | CYS148 | |
A | HIS185 | |
A | CYS188 | |
A | CYS213 | |
A | CYS219 | |
L | ILE531 | |
A | CYS228 | |
A | CYS246 | |
A | CYS249 | |
C | CYS17 | |
C | CYS20 | |
C | CYS112 | |
C | CYS148 | |
C | HIS185 | |
C | CYS188 | |
C | CYS213 | |
B | GLY66 | |
C | CYS219 | |
C | CYS228 | |
C | CYS246 | |
C | CYS249 | |
E | CYS17 | |
E | CYS20 | |
E | CYS112 | |
E | CYS148 | |
E | HIS185 | |
E | CYS188 | |
B | ILE531 | |
E | CYS213 | |
E | CYS219 | |
E | CYS228 | |
E | CYS246 | |
E | CYS249 | |
G | CYS17 | |
G | CYS20 | |
G | CYS112 | |
G | CYS148 | |
G | HIS185 | |
D | GLY66 | |
G | CYS188 | |
G | CYS213 | |
G | CYS219 | |
G | CYS228 | |
G | CYS246 | |
G | CYS249 | |
I | CYS17 | |
I | CYS20 | |
I | CYS112 | |
I | CYS148 | |
D | ILE531 | |
I | HIS185 | |
I | CYS188 | |
I | CYS213 | |
I | CYS219 | |
I | CYS228 | |
I | CYS246 | |
I | CYS249 | |
F | GLY66 | |
F | ILE531 | |
H | GLY66 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: |
Chain | Residue | Details |
L | THR69 | |
H | GLY534 | |
J | THR69 | |
J | GLY534 | |
L | GLY534 | |
B | THR69 | |
B | GLY534 | |
D | THR69 | |
D | GLY534 | |
F | THR69 | |
F | GLY534 | |
H | THR69 |
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 |
L | GLY19 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
L | GLY66 | activator, metal ligand |
L | THR69 | activator, electrostatic stabiliser, metal ligand |
L | ALA73 | electrostatic stabiliser, hydrogen bond donor |
L | GLY464 | electrostatic stabiliser, hydrogen bond donor |
L | THR487 | electrostatic stabiliser, hydrogen bond donor |
L | ILE531 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
L | GLY534 | activator, electrostatic stabiliser, metal ligand |
site_id | MCSA2 |
Number of Residues | 8 |
Details | M-CSA 126 |
Chain | Residue | Details |
B | GLY19 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
B | GLY66 | activator, metal ligand |
B | THR69 | activator, electrostatic stabiliser, metal ligand |
B | ALA73 | electrostatic stabiliser, hydrogen bond donor |
B | GLY464 | electrostatic stabiliser, hydrogen bond donor |
B | THR487 | electrostatic stabiliser, hydrogen bond donor |
B | ILE531 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
B | GLY534 | activator, electrostatic stabiliser, metal ligand |
site_id | MCSA3 |
Number of Residues | 8 |
Details | M-CSA 126 |
Chain | Residue | Details |
D | GLY19 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
D | GLY66 | activator, metal ligand |
D | THR69 | activator, electrostatic stabiliser, metal ligand |
D | ALA73 | electrostatic stabiliser, hydrogen bond donor |
D | GLY464 | electrostatic stabiliser, hydrogen bond donor |
D | THR487 | electrostatic stabiliser, hydrogen bond donor |
D | ILE531 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
D | GLY534 | activator, electrostatic stabiliser, metal ligand |
site_id | MCSA4 |
Number of Residues | 8 |
Details | M-CSA 126 |
Chain | Residue | Details |
F | GLY19 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
F | GLY66 | activator, metal ligand |
F | THR69 | activator, electrostatic stabiliser, metal ligand |
F | ALA73 | electrostatic stabiliser, hydrogen bond donor |
F | GLY464 | electrostatic stabiliser, hydrogen bond donor |
F | THR487 | electrostatic stabiliser, hydrogen bond donor |
F | ILE531 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
F | GLY534 | activator, electrostatic stabiliser, metal ligand |
site_id | MCSA5 |
Number of Residues | 8 |
Details | M-CSA 126 |
Chain | Residue | Details |
H | GLY19 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
H | GLY66 | activator, metal ligand |
H | THR69 | activator, electrostatic stabiliser, metal ligand |
H | ALA73 | electrostatic stabiliser, hydrogen bond donor |
H | GLY464 | electrostatic stabiliser, hydrogen bond donor |
H | THR487 | electrostatic stabiliser, hydrogen bond donor |
H | ILE531 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
H | GLY534 | activator, electrostatic stabiliser, metal ligand |
site_id | MCSA6 |
Number of Residues | 8 |
Details | M-CSA 126 |
Chain | Residue | Details |
J | GLY19 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
J | GLY66 | activator, metal ligand |
J | THR69 | activator, electrostatic stabiliser, metal ligand |
J | ALA73 | electrostatic stabiliser, hydrogen bond donor |
J | GLY464 | electrostatic stabiliser, hydrogen bond donor |
J | THR487 | electrostatic stabiliser, hydrogen bond donor |
J | ILE531 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
J | GLY534 | activator, electrostatic stabiliser, metal ligand |