1E7P
QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005886 | cellular_component | plasma membrane |
A | 0008177 | molecular_function | succinate dehydrogenase (quinone) activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
A | 0022900 | biological_process | electron transport chain |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 0070469 | cellular_component | respirasome |
B | 0005886 | cellular_component | plasma membrane |
B | 0006099 | biological_process | tricarboxylic acid cycle |
B | 0009055 | molecular_function | electron transfer activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0051536 | molecular_function | iron-sulfur cluster binding |
B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
B | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
B | 0070469 | cellular_component | respirasome |
C | 0005886 | cellular_component | plasma membrane |
C | 0006099 | biological_process | tricarboxylic acid cycle |
C | 0016020 | cellular_component | membrane |
C | 0046872 | molecular_function | metal ion binding |
C | 0070469 | cellular_component | respirasome |
D | 0005886 | cellular_component | plasma membrane |
D | 0008177 | molecular_function | succinate dehydrogenase (quinone) activity |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
D | 0022900 | biological_process | electron transport chain |
D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
D | 0070469 | cellular_component | respirasome |
E | 0005886 | cellular_component | plasma membrane |
E | 0006099 | biological_process | tricarboxylic acid cycle |
E | 0009055 | molecular_function | electron transfer activity |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0046872 | molecular_function | metal ion binding |
E | 0051536 | molecular_function | iron-sulfur cluster binding |
E | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
E | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
E | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
E | 0070469 | cellular_component | respirasome |
F | 0005886 | cellular_component | plasma membrane |
F | 0006099 | biological_process | tricarboxylic acid cycle |
F | 0016020 | cellular_component | membrane |
F | 0046872 | molecular_function | metal ion binding |
F | 0070469 | cellular_component | respirasome |
G | 0005886 | cellular_component | plasma membrane |
G | 0008177 | molecular_function | succinate dehydrogenase (quinone) activity |
G | 0016491 | molecular_function | oxidoreductase activity |
G | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
G | 0022900 | biological_process | electron transport chain |
G | 0050660 | molecular_function | flavin adenine dinucleotide binding |
G | 0070469 | cellular_component | respirasome |
H | 0005886 | cellular_component | plasma membrane |
H | 0006099 | biological_process | tricarboxylic acid cycle |
H | 0009055 | molecular_function | electron transfer activity |
H | 0016491 | molecular_function | oxidoreductase activity |
H | 0046872 | molecular_function | metal ion binding |
H | 0051536 | molecular_function | iron-sulfur cluster binding |
H | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
H | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
H | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
H | 0070469 | cellular_component | respirasome |
I | 0005886 | cellular_component | plasma membrane |
I | 0006099 | biological_process | tricarboxylic acid cycle |
I | 0016020 | cellular_component | membrane |
I | 0046872 | molecular_function | metal ion binding |
I | 0070469 | cellular_component | respirasome |
J | 0005886 | cellular_component | plasma membrane |
J | 0008177 | molecular_function | succinate dehydrogenase (quinone) activity |
J | 0016491 | molecular_function | oxidoreductase activity |
J | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
J | 0022900 | biological_process | electron transport chain |
J | 0050660 | molecular_function | flavin adenine dinucleotide binding |
J | 0070469 | cellular_component | respirasome |
K | 0005886 | cellular_component | plasma membrane |
K | 0006099 | biological_process | tricarboxylic acid cycle |
K | 0009055 | molecular_function | electron transfer activity |
K | 0016491 | molecular_function | oxidoreductase activity |
K | 0046872 | molecular_function | metal ion binding |
K | 0051536 | molecular_function | iron-sulfur cluster binding |
K | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
K | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
K | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
K | 0070469 | cellular_component | respirasome |
L | 0005886 | cellular_component | plasma membrane |
L | 0006099 | biological_process | tricarboxylic acid cycle |
L | 0016020 | cellular_component | membrane |
L | 0046872 | molecular_function | metal ion binding |
L | 0070469 | cellular_component | respirasome |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE FAD A 701 |
Chain | Residue |
A | GLY12 |
A | SER44 |
A | ALA46 |
A | ALA47 |
A | GLN48 |
A | GLY49 |
A | GLY50 |
A | ALA181 |
A | ALA215 |
A | THR216 |
A | GLY217 |
A | GLY13 |
A | THR227 |
A | ASN228 |
A | THR235 |
A | LEU267 |
A | HIS369 |
A | TYR370 |
A | GLU393 |
A | ARG404 |
A | GLY407 |
A | SER409 |
A | GLY14 |
A | VAL410 |
A | MLA702 |
A | LEU15 |
A | ALA16 |
A | SER35 |
A | LEU36 |
A | SER42 |
A | HIS43 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE MLA A 702 |
Chain | Residue |
A | PHE141 |
A | HIS257 |
A | LEU267 |
A | THR269 |
A | GLU270 |
A | HIS369 |
A | ARG404 |
A | GLY407 |
A | FAD701 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A 703 |
Chain | Residue |
A | TYR370 |
A | SER371 |
A | MET372 |
A | GLU393 |
A | ALA395 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE FES B 301 |
Chain | Residue |
B | CYS57 |
B | ARG58 |
B | GLY60 |
B | ILE61 |
B | CYS62 |
B | GLY63 |
B | CYS65 |
B | CYS77 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE F3S B 302 |
Chain | Residue |
B | CYS161 |
B | THR163 |
B | CYS208 |
B | THR210 |
B | LEU211 |
B | LEU212 |
B | ALA213 |
B | CYS214 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SF4 B 303 |
Chain | Residue |
B | CYS151 |
B | ILE152 |
B | GLU153 |
B | CYS154 |
B | GLY155 |
B | CYS157 |
B | ALA174 |
B | CYS218 |
site_id | AC7 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE HEM C 301 |
Chain | Residue |
C | GLN30 |
C | SER31 |
C | GLY34 |
C | LEU37 |
C | PHE90 |
C | HIS93 |
C | ALA94 |
C | ALA97 |
C | LYS100 |
C | TRP126 |
C | GLN129 |
C | GLY133 |
C | MET136 |
C | PHE137 |
C | HIS182 |
C | GLY183 |
C | GLY186 |
C | LEU190 |
C | LYS193 |
site_id | AC8 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE HEM C 302 |
Chain | Residue |
C | TYR172 |
C | LEU175 |
C | LEU176 |
C | VAL179 |
C | GLY224 |
C | PHE228 |
C | PHE40 |
C | MET41 |
C | HIS44 |
C | VAL48 |
C | LEU82 |
C | ALA83 |
C | HIS143 |
C | MET147 |
C | ILE154 |
C | SER159 |
C | ARG162 |
site_id | AC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE LMT C 303 |
Chain | Residue |
C | MET22 |
C | PHE95 |
C | MET98 |
F | PHE101 |
F | PRO102 |
F | TYR105 |
F | TYR108 |
F | ALA130 |
F | MET131 |
site_id | BC1 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE FAD D 701 |
Chain | Residue |
D | GLY12 |
D | GLY13 |
D | GLY14 |
D | LEU15 |
D | ALA16 |
D | SER35 |
D | LEU36 |
D | SER42 |
D | HIS43 |
D | SER44 |
D | ALA46 |
D | ALA47 |
D | GLN48 |
D | GLY49 |
D | GLY50 |
D | ALA181 |
D | ALA215 |
D | THR216 |
D | GLY217 |
D | THR227 |
D | ASN228 |
D | THR235 |
D | LEU267 |
D | HIS369 |
D | TYR370 |
D | GLU393 |
D | ARG404 |
D | GLY407 |
D | SER409 |
D | VAL410 |
D | MLA702 |
site_id | BC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE MLA D 702 |
Chain | Residue |
D | PHE141 |
D | HIS257 |
D | LEU267 |
D | THR269 |
D | GLU270 |
D | HIS369 |
D | ARG404 |
D | GLY407 |
D | FAD701 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA D 703 |
Chain | Residue |
D | TYR370 |
D | SER371 |
D | MET372 |
D | GLU393 |
D | ALA395 |
site_id | BC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE FES E 301 |
Chain | Residue |
E | CYS57 |
E | ARG58 |
E | GLY60 |
E | ILE61 |
E | CYS62 |
E | GLY63 |
E | CYS65 |
E | CYS77 |
site_id | BC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE F3S E 302 |
Chain | Residue |
E | CYS161 |
E | THR163 |
E | CYS208 |
E | THR210 |
E | LEU211 |
E | LEU212 |
E | ALA213 |
E | CYS214 |
site_id | BC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SF4 E 303 |
Chain | Residue |
E | CYS151 |
E | ILE152 |
E | GLU153 |
E | CYS154 |
E | GLY155 |
E | CYS157 |
E | ALA174 |
E | CYS218 |
site_id | BC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE LMT F 301 |
Chain | Residue |
C | PHE101 |
C | PRO102 |
C | TYR105 |
C | TYR108 |
C | ALA130 |
C | MET131 |
F | MET22 |
F | PHE95 |
F | MET98 |
site_id | BC8 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE HEM F 302 |
Chain | Residue |
F | GLN30 |
F | SER31 |
F | GLY34 |
F | LEU37 |
F | PHE90 |
F | HIS93 |
F | ALA94 |
F | ALA97 |
F | LYS100 |
F | TRP126 |
F | GLN129 |
F | GLY133 |
F | MET136 |
F | PHE137 |
F | HIS182 |
F | GLY183 |
F | GLY186 |
F | LEU190 |
F | LYS193 |
site_id | BC9 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE HEM F 303 |
Chain | Residue |
F | PHE40 |
F | MET41 |
F | HIS44 |
F | VAL48 |
F | LEU82 |
F | ALA83 |
F | HIS143 |
F | MET147 |
F | ILE154 |
F | SER159 |
F | ARG162 |
F | TYR172 |
F | LEU175 |
F | LEU176 |
F | VAL179 |
F | GLY224 |
F | PHE228 |
site_id | CC1 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE FAD G 701 |
Chain | Residue |
G | GLY12 |
G | GLY13 |
G | GLY14 |
G | LEU15 |
G | ALA16 |
G | SER35 |
G | LEU36 |
G | SER42 |
G | HIS43 |
G | SER44 |
G | ALA46 |
G | ALA47 |
G | GLN48 |
G | GLY49 |
G | GLY50 |
G | ALA181 |
G | ALA215 |
G | THR216 |
G | GLY217 |
G | THR227 |
G | ASN228 |
G | THR235 |
G | LEU267 |
G | HIS369 |
G | TYR370 |
G | GLU393 |
G | ARG404 |
G | GLY407 |
G | SER409 |
G | VAL410 |
G | MLA702 |
site_id | CC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE MLA G 702 |
Chain | Residue |
G | PHE141 |
G | HIS257 |
G | LEU267 |
G | THR269 |
G | GLU270 |
G | HIS369 |
G | ARG404 |
G | GLY407 |
G | FAD701 |
site_id | CC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA G 703 |
Chain | Residue |
G | TYR370 |
G | SER371 |
G | MET372 |
G | GLU393 |
G | ALA395 |
site_id | CC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE FES H 301 |
Chain | Residue |
H | CYS57 |
H | ARG58 |
H | GLY60 |
H | ILE61 |
H | CYS62 |
H | GLY63 |
H | CYS65 |
H | CYS77 |
site_id | CC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE F3S H 302 |
Chain | Residue |
H | CYS161 |
H | THR163 |
H | CYS208 |
H | THR210 |
H | LEU211 |
H | LEU212 |
H | ALA213 |
H | CYS214 |
site_id | CC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SF4 H 303 |
Chain | Residue |
H | CYS151 |
H | ILE152 |
H | GLU153 |
H | CYS154 |
H | GLY155 |
H | CYS157 |
H | ALA174 |
H | CYS218 |
site_id | CC7 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE HEM I 301 |
Chain | Residue |
I | GLN30 |
I | SER31 |
I | GLY34 |
I | LEU37 |
I | PHE90 |
I | HIS93 |
I | ALA94 |
I | ALA97 |
I | LYS100 |
I | TRP126 |
I | GLN129 |
I | GLY133 |
I | MET136 |
I | PHE137 |
I | HIS182 |
I | GLY183 |
I | GLY186 |
I | LEU190 |
I | LYS193 |
site_id | CC8 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE HEM I 302 |
Chain | Residue |
I | PHE40 |
I | MET41 |
I | HIS44 |
I | VAL48 |
I | LEU82 |
I | ALA83 |
I | HIS143 |
I | MET147 |
I | ILE154 |
I | SER159 |
I | ARG162 |
I | TYR172 |
I | LEU175 |
I | LEU176 |
I | VAL179 |
I | GLY224 |
I | PHE228 |
site_id | CC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE LMT I 303 |
Chain | Residue |
I | MET22 |
I | PHE95 |
I | MET98 |
L | PHE101 |
L | PRO102 |
L | TYR105 |
L | TYR108 |
L | ALA130 |
L | MET131 |
site_id | DC1 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE FAD J 701 |
Chain | Residue |
J | GLY12 |
J | GLY13 |
J | GLY14 |
J | LEU15 |
J | ALA16 |
J | SER35 |
J | LEU36 |
J | SER42 |
J | HIS43 |
J | SER44 |
J | ALA46 |
J | ALA47 |
J | GLN48 |
J | GLY49 |
J | GLY50 |
J | ALA181 |
J | ALA215 |
J | THR216 |
J | GLY217 |
J | THR227 |
J | ASN228 |
J | THR235 |
J | LEU267 |
J | HIS369 |
J | TYR370 |
J | GLU393 |
J | ARG404 |
J | GLY407 |
J | SER409 |
J | VAL410 |
J | MLA702 |
site_id | DC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE MLA J 702 |
Chain | Residue |
J | PHE141 |
J | HIS257 |
J | LEU267 |
J | THR269 |
J | GLU270 |
J | HIS369 |
J | ARG404 |
J | GLY407 |
J | FAD701 |
site_id | DC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA J 703 |
Chain | Residue |
J | TYR370 |
J | SER371 |
J | MET372 |
J | GLU393 |
J | ALA395 |
site_id | DC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE FES K 301 |
Chain | Residue |
K | CYS57 |
K | ARG58 |
K | GLY60 |
K | ILE61 |
K | CYS62 |
K | GLY63 |
K | CYS65 |
K | CYS77 |
site_id | DC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE F3S K 302 |
Chain | Residue |
K | CYS161 |
K | THR163 |
K | CYS208 |
K | THR210 |
K | LEU211 |
K | LEU212 |
K | ALA213 |
K | CYS214 |
site_id | DC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SF4 K 303 |
Chain | Residue |
K | CYS151 |
K | ILE152 |
K | GLU153 |
K | CYS154 |
K | GLY155 |
K | CYS157 |
K | ALA174 |
K | CYS218 |
site_id | DC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE LMT L 301 |
Chain | Residue |
I | PHE101 |
I | PRO102 |
I | TYR105 |
I | TYR108 |
I | ALA130 |
I | MET131 |
L | MET22 |
L | PHE95 |
L | MET98 |
site_id | DC8 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE HEM L 302 |
Chain | Residue |
L | GLN30 |
L | SER31 |
L | GLY34 |
L | LEU37 |
L | PHE90 |
L | HIS93 |
L | ALA94 |
L | ALA97 |
L | LYS100 |
L | TRP126 |
L | GLN129 |
L | GLY133 |
L | MET136 |
L | PHE137 |
L | HIS182 |
L | GLY183 |
L | GLY186 |
L | LEU190 |
L | LYS193 |
site_id | DC9 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE HEM L 303 |
Chain | Residue |
L | PHE40 |
L | MET41 |
L | HIS44 |
L | VAL48 |
L | LEU82 |
L | ALA83 |
L | HIS143 |
L | MET147 |
L | ILE154 |
L | SER159 |
L | ARG162 |
L | TYR172 |
L | LEU175 |
L | LEU176 |
L | VAL179 |
L | GLY224 |
L | PHE228 |
Functional Information from PROSITE/UniProt
site_id | PS00197 |
Number of Residues | 9 |
Details | 2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CRAGICGSC |
Chain | Residue | Details |
B | CYS57-CYS65 |
site_id | PS00198 |
Number of Residues | 12 |
Details | 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiECGcCIaACG |
Chain | Residue | Details |
B | CYS151-GLY162 |
site_id | PS00504 |
Number of Residues | 10 |
Details | FRD_SDH_FAD_BINDING Fumarate reductase / succinate dehydrogenase FAD-binding site. RSHSaaAqGG |
Chain | Residue | Details |
A | ARG41-GLY50 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 116 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:10586875 |
Chain | Residue | Details |
C | MET1-GLN30 | |
B | CYS214 | |
B | CYS218 | |
E | CYS57 | |
E | CYS62 | |
E | CYS65 | |
E | CYS77 | |
E | CYS151 | |
E | CYS154 | |
E | CYS157 | |
E | CYS161 | |
F | MET1-GLN30 | |
E | CYS208 | |
E | CYS214 | |
E | CYS218 | |
H | CYS57 | |
H | CYS62 | |
H | CYS65 | |
H | CYS77 | |
H | CYS151 | |
H | CYS154 | |
H | CYS157 | |
I | MET1-GLN30 | |
H | CYS161 | |
H | CYS208 | |
H | CYS214 | |
H | CYS218 | |
K | CYS57 | |
K | CYS62 | |
K | CYS65 | |
K | CYS77 | |
K | CYS151 | |
K | CYS154 | |
L | MET1-GLN30 | |
K | CYS157 | |
K | CYS161 | |
K | CYS208 | |
K | CYS214 | |
K | CYS218 | |
B | CYS151 | |
B | CYS154 | |
B | CYS157 | |
B | CYS161 | |
B | CYS208 |
site_id | SWS_FT_FI2 |
Number of Residues | 444 |
Details | TRANSMEM: Helical |
Chain | Residue | Details |
C | SER31-LEU52 | |
F | ALA207-ALA230 | |
I | SER31-LEU52 | |
I | ILE77-MET98 | |
I | LEU125-THR149 | |
I | GLU166-TYR188 | |
I | ALA207-ALA230 | |
L | SER31-LEU52 | |
L | ILE77-MET98 | |
L | LEU125-THR149 | |
L | GLU166-TYR188 | |
C | ILE77-MET98 | |
L | ALA207-ALA230 | |
C | LEU125-THR149 | |
C | GLU166-TYR188 | |
C | ALA207-ALA230 | |
F | SER31-LEU52 | |
F | ILE77-MET98 | |
F | LEU125-THR149 | |
F | GLU166-TYR188 |
site_id | SWS_FT_FI3 |
Number of Residues | 152 |
Details | TOPO_DOM: Periplasmic |
Chain | Residue | Details |
C | LEU53-PRO76 | |
C | GLN150-SER165 | |
F | LEU53-PRO76 | |
F | GLN150-SER165 | |
I | LEU53-PRO76 | |
I | GLN150-SER165 | |
L | LEU53-PRO76 | |
L | GLN150-SER165 |
site_id | SWS_FT_FI4 |
Number of Residues | 168 |
Details | TOPO_DOM: Cytoplasmic |
Chain | Residue | Details |
C | ARG99-THR124 | |
C | ARG189-ARG206 | |
F | ARG99-THR124 | |
F | ARG189-ARG206 | |
I | ARG99-THR124 | |
I | ARG189-ARG206 | |
L | ARG99-THR124 | |
L | ARG189-ARG206 |
site_id | SWS_FT_FI5 |
Number of Residues | 100 |
Details | TOPO_DOM: Periplasmic => ECO:0000269|PubMed:10586875 |
Chain | Residue | Details |
C | TYR231-ARG256 | |
F | TYR231-ARG256 | |
I | TYR231-ARG256 | |
L | TYR231-ARG256 |
site_id | SWS_FT_FI6 |
Number of Residues | 16 |
Details | BINDING: axial binding residue => ECO:0000269|PubMed:10586875, ECO:0000269|PubMed:11248702, ECO:0007744|PDB:1E7P, ECO:0007744|PDB:1QLB, ECO:0007744|PDB:2BS2, ECO:0007744|PDB:2BS3, ECO:0007744|PDB:2BS4 |
Chain | Residue | Details |
C | HIS44 | |
I | HIS93 | |
I | HIS143 | |
I | HIS182 | |
L | HIS44 | |
L | HIS93 | |
L | HIS143 | |
L | HIS182 | |
C | HIS93 | |
C | HIS143 | |
C | HIS182 | |
F | HIS44 | |
F | HIS93 | |
F | HIS143 | |
F | HIS182 | |
I | HIS44 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1d4c |
Chain | Residue | Details |
A | HIS257 | |
A | ARG404 | |
A | HIS369 | |
A | ARG301 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1d4c |
Chain | Residue | Details |
D | HIS257 | |
D | ARG404 | |
D | HIS369 | |
D | ARG301 |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1d4c |
Chain | Residue | Details |
G | HIS257 | |
G | ARG404 | |
G | HIS369 | |
G | ARG301 |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1d4c |
Chain | Residue | Details |
J | HIS257 | |
J | ARG404 | |
J | HIS369 | |
J | ARG301 |