6C4A
Crystal structure of 3-nitropropionate modified isocitrate lyase from Mycobacterium tuberculosis with pyruvate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004451 | molecular_function | isocitrate lyase activity |
A | 0005576 | cellular_component | extracellular region |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0006097 | biological_process | glyoxylate cycle |
A | 0006099 | biological_process | tricarboxylic acid cycle |
A | 0006102 | biological_process | isocitrate metabolic process |
A | 0016829 | molecular_function | lyase activity |
A | 0019752 | biological_process | carboxylic acid metabolic process |
A | 0035375 | molecular_function | zymogen binding |
A | 0046421 | molecular_function | methylisocitrate lyase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0052572 | biological_process | response to host immune response |
A | 0071456 | biological_process | cellular response to hypoxia |
B | 0003824 | molecular_function | catalytic activity |
B | 0004451 | molecular_function | isocitrate lyase activity |
B | 0005576 | cellular_component | extracellular region |
B | 0005829 | cellular_component | cytosol |
B | 0005886 | cellular_component | plasma membrane |
B | 0006097 | biological_process | glyoxylate cycle |
B | 0006099 | biological_process | tricarboxylic acid cycle |
B | 0006102 | biological_process | isocitrate metabolic process |
B | 0016829 | molecular_function | lyase activity |
B | 0019752 | biological_process | carboxylic acid metabolic process |
B | 0035375 | molecular_function | zymogen binding |
B | 0046421 | molecular_function | methylisocitrate lyase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0052572 | biological_process | response to host immune response |
B | 0071456 | biological_process | cellular response to hypoxia |
C | 0003824 | molecular_function | catalytic activity |
C | 0004451 | molecular_function | isocitrate lyase activity |
C | 0005576 | cellular_component | extracellular region |
C | 0005829 | cellular_component | cytosol |
C | 0005886 | cellular_component | plasma membrane |
C | 0006097 | biological_process | glyoxylate cycle |
C | 0006099 | biological_process | tricarboxylic acid cycle |
C | 0006102 | biological_process | isocitrate metabolic process |
C | 0016829 | molecular_function | lyase activity |
C | 0019752 | biological_process | carboxylic acid metabolic process |
C | 0035375 | molecular_function | zymogen binding |
C | 0046421 | molecular_function | methylisocitrate lyase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0052572 | biological_process | response to host immune response |
C | 0071456 | biological_process | cellular response to hypoxia |
D | 0003824 | molecular_function | catalytic activity |
D | 0004451 | molecular_function | isocitrate lyase activity |
D | 0005576 | cellular_component | extracellular region |
D | 0005829 | cellular_component | cytosol |
D | 0005886 | cellular_component | plasma membrane |
D | 0006097 | biological_process | glyoxylate cycle |
D | 0006099 | biological_process | tricarboxylic acid cycle |
D | 0006102 | biological_process | isocitrate metabolic process |
D | 0016829 | molecular_function | lyase activity |
D | 0019752 | biological_process | carboxylic acid metabolic process |
D | 0035375 | molecular_function | zymogen binding |
D | 0046421 | molecular_function | methylisocitrate lyase activity |
D | 0046872 | molecular_function | metal ion binding |
D | 0052572 | biological_process | response to host immune response |
D | 0071456 | biological_process | cellular response to hypoxia |
E | 0003824 | molecular_function | catalytic activity |
E | 0004451 | molecular_function | isocitrate lyase activity |
E | 0005576 | cellular_component | extracellular region |
E | 0005829 | cellular_component | cytosol |
E | 0005886 | cellular_component | plasma membrane |
E | 0006097 | biological_process | glyoxylate cycle |
E | 0006099 | biological_process | tricarboxylic acid cycle |
E | 0006102 | biological_process | isocitrate metabolic process |
E | 0016829 | molecular_function | lyase activity |
E | 0019752 | biological_process | carboxylic acid metabolic process |
E | 0035375 | molecular_function | zymogen binding |
E | 0046421 | molecular_function | methylisocitrate lyase activity |
E | 0046872 | molecular_function | metal ion binding |
E | 0052572 | biological_process | response to host immune response |
E | 0071456 | biological_process | cellular response to hypoxia |
F | 0003824 | molecular_function | catalytic activity |
F | 0004451 | molecular_function | isocitrate lyase activity |
F | 0005576 | cellular_component | extracellular region |
F | 0005829 | cellular_component | cytosol |
F | 0005886 | cellular_component | plasma membrane |
F | 0006097 | biological_process | glyoxylate cycle |
F | 0006099 | biological_process | tricarboxylic acid cycle |
F | 0006102 | biological_process | isocitrate metabolic process |
F | 0016829 | molecular_function | lyase activity |
F | 0019752 | biological_process | carboxylic acid metabolic process |
F | 0035375 | molecular_function | zymogen binding |
F | 0046421 | molecular_function | methylisocitrate lyase activity |
F | 0046872 | molecular_function | metal ion binding |
F | 0052572 | biological_process | response to host immune response |
F | 0071456 | biological_process | cellular response to hypoxia |
G | 0003824 | molecular_function | catalytic activity |
G | 0004451 | molecular_function | isocitrate lyase activity |
G | 0005576 | cellular_component | extracellular region |
G | 0005829 | cellular_component | cytosol |
G | 0005886 | cellular_component | plasma membrane |
G | 0006097 | biological_process | glyoxylate cycle |
G | 0006099 | biological_process | tricarboxylic acid cycle |
G | 0006102 | biological_process | isocitrate metabolic process |
G | 0016829 | molecular_function | lyase activity |
G | 0019752 | biological_process | carboxylic acid metabolic process |
G | 0035375 | molecular_function | zymogen binding |
G | 0046421 | molecular_function | methylisocitrate lyase activity |
G | 0046872 | molecular_function | metal ion binding |
G | 0052572 | biological_process | response to host immune response |
G | 0071456 | biological_process | cellular response to hypoxia |
H | 0003824 | molecular_function | catalytic activity |
H | 0004451 | molecular_function | isocitrate lyase activity |
H | 0005576 | cellular_component | extracellular region |
H | 0005829 | cellular_component | cytosol |
H | 0005886 | cellular_component | plasma membrane |
H | 0006097 | biological_process | glyoxylate cycle |
H | 0006099 | biological_process | tricarboxylic acid cycle |
H | 0006102 | biological_process | isocitrate metabolic process |
H | 0016829 | molecular_function | lyase activity |
H | 0019752 | biological_process | carboxylic acid metabolic process |
H | 0035375 | molecular_function | zymogen binding |
H | 0046421 | molecular_function | methylisocitrate lyase activity |
H | 0046872 | molecular_function | metal ion binding |
H | 0052572 | biological_process | response to host immune response |
H | 0071456 | biological_process | cellular response to hypoxia |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | binding site for residue PYR A 501 |
Chain | Residue |
A | TYR89 |
A | THR347 |
A | MG502 |
A | HOH611 |
A | HOH620 |
A | HOH650 |
A | SER91 |
A | GLY92 |
A | TRP93 |
A | ASP153 |
A | HIS180 |
A | EJA191 |
A | ARG228 |
A | TRP283 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue MG A 502 |
Chain | Residue |
A | ASP153 |
A | PYR501 |
A | HOH611 |
A | HOH620 |
A | HOH650 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue MG A 503 |
Chain | Residue |
A | ALA276 |
A | ALA279 |
A | GLN308 |
A | HOH633 |
A | HOH848 |
A | HOH855 |
site_id | AC4 |
Number of Residues | 10 |
Details | binding site for residue 3NP B 502 |
Chain | Residue |
A | TYR356 |
A | SER357 |
A | LEU376 |
A | ARG379 |
B | TYR356 |
B | SER357 |
B | LEU376 |
B | ARG379 |
B | HOH601 |
B | HOH648 |
site_id | AC5 |
Number of Residues | 14 |
Details | binding site for residue PYR B 503 |
Chain | Residue |
B | TYR89 |
B | SER91 |
B | GLY92 |
B | TRP93 |
B | ASP153 |
B | HIS180 |
B | EJA191 |
B | ARG228 |
B | TRP283 |
B | THR347 |
B | MG504 |
B | HOH606 |
B | HOH612 |
B | HOH661 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue MG B 504 |
Chain | Residue |
B | ASP153 |
B | PYR503 |
B | HOH606 |
B | HOH612 |
B | HOH661 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue MG B 505 |
Chain | Residue |
B | ALA276 |
B | ALA279 |
B | GLN308 |
B | HOH734 |
B | HOH811 |
B | HOH826 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue PEG B 506 |
Chain | Residue |
B | LEU63 |
B | GLU64 |
site_id | AC9 |
Number of Residues | 14 |
Details | binding site for residue PYR C 501 |
Chain | Residue |
C | TYR89 |
C | SER91 |
C | GLY92 |
C | TRP93 |
C | ASP153 |
C | HIS180 |
C | EJA191 |
C | ARG228 |
C | TRP283 |
C | THR347 |
C | MG502 |
C | HOH619 |
C | HOH625 |
C | HOH634 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue MG C 502 |
Chain | Residue |
C | ASP153 |
C | PYR501 |
C | HOH619 |
C | HOH625 |
C | HOH634 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue MG C 503 |
Chain | Residue |
C | ALA276 |
C | ALA279 |
C | GLN308 |
C | HOH744 |
C | HOH819 |
C | HOH872 |
site_id | AD3 |
Number of Residues | 2 |
Details | binding site for residue PEG C 504 |
Chain | Residue |
C | TRP65 |
C | HOH678 |
site_id | AD4 |
Number of Residues | 10 |
Details | binding site for residue 3NP C 505 |
Chain | Residue |
C | TYR356 |
C | SER357 |
C | ARG379 |
C | HOH601 |
C | HOH626 |
D | TYR356 |
D | SER357 |
D | LEU376 |
D | ARG379 |
D | HOH646 |
site_id | AD5 |
Number of Residues | 14 |
Details | binding site for residue PYR D 501 |
Chain | Residue |
D | TYR89 |
D | SER91 |
D | GLY92 |
D | TRP93 |
D | ASP153 |
D | HIS180 |
D | EJA191 |
D | ARG228 |
D | TRP283 |
D | THR347 |
D | MG502 |
D | HOH605 |
D | HOH612 |
D | HOH653 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue MG D 502 |
Chain | Residue |
D | ASP153 |
D | PYR501 |
D | HOH605 |
D | HOH612 |
D | HOH653 |
site_id | AD7 |
Number of Residues | 6 |
Details | binding site for residue MG D 503 |
Chain | Residue |
D | ALA276 |
D | ALA279 |
D | GLN308 |
D | HOH771 |
D | HOH836 |
D | HOH849 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue PEG D 504 |
Chain | Residue |
C | ALA366 |
C | GLN369 |
D | TRP65 |
site_id | AD9 |
Number of Residues | 14 |
Details | binding site for residue PYR E 501 |
Chain | Residue |
E | TYR89 |
E | SER91 |
E | GLY92 |
E | TRP93 |
E | ASP153 |
E | HIS180 |
E | EJA191 |
E | ARG228 |
E | TRP283 |
E | THR347 |
E | MG502 |
E | HOH608 |
E | HOH636 |
E | HOH664 |
site_id | AE1 |
Number of Residues | 5 |
Details | binding site for residue MG E 502 |
Chain | Residue |
E | ASP153 |
E | PYR501 |
E | HOH608 |
E | HOH636 |
E | HOH664 |
site_id | AE2 |
Number of Residues | 6 |
Details | binding site for residue MG E 503 |
Chain | Residue |
E | ALA276 |
E | ALA279 |
E | GLN308 |
E | HOH662 |
E | HOH920 |
E | HOH928 |
site_id | AE3 |
Number of Residues | 3 |
Details | binding site for residue PEG E 504 |
Chain | Residue |
E | TRP65 |
F | GLN367 |
F | GLN369 |
site_id | AE4 |
Number of Residues | 8 |
Details | binding site for residue EPE F 501 |
Chain | Residue |
E | TYR356 |
F | TYR356 |
F | SER357 |
F | ASP360 |
F | ARG379 |
F | HOH601 |
F | HOH734 |
F | HOH754 |
site_id | AE5 |
Number of Residues | 14 |
Details | binding site for residue PYR F 502 |
Chain | Residue |
F | TYR89 |
F | SER91 |
F | GLY92 |
F | TRP93 |
F | ASP153 |
F | HIS180 |
F | EJA191 |
F | ARG228 |
F | TRP283 |
F | THR347 |
F | MG503 |
F | HOH620 |
F | HOH629 |
F | HOH643 |
site_id | AE6 |
Number of Residues | 5 |
Details | binding site for residue MG F 503 |
Chain | Residue |
F | ASP153 |
F | PYR502 |
F | HOH620 |
F | HOH629 |
F | HOH643 |
site_id | AE7 |
Number of Residues | 6 |
Details | binding site for residue MG F 504 |
Chain | Residue |
F | HOH624 |
F | HOH667 |
F | HOH829 |
F | HOH933 |
G | HOH808 |
G | HOH893 |
site_id | AE8 |
Number of Residues | 6 |
Details | binding site for residue MG F 505 |
Chain | Residue |
F | ALA276 |
F | ALA279 |
F | GLN308 |
F | HOH692 |
F | HOH910 |
F | HOH914 |
site_id | AE9 |
Number of Residues | 3 |
Details | binding site for residue PEG F 506 |
Chain | Residue |
F | LEU63 |
F | TRP65 |
F | ASN67 |
site_id | AF1 |
Number of Residues | 14 |
Details | binding site for residue PYR G 501 |
Chain | Residue |
G | TYR89 |
G | SER91 |
G | GLY92 |
G | TRP93 |
G | ASP153 |
G | HIS180 |
G | EJA191 |
G | ARG228 |
G | TRP283 |
G | THR347 |
G | MG502 |
G | HOH603 |
G | HOH629 |
G | HOH680 |
site_id | AF2 |
Number of Residues | 5 |
Details | binding site for residue MG G 502 |
Chain | Residue |
G | ASP153 |
G | PYR501 |
G | HOH603 |
G | HOH629 |
G | HOH680 |
site_id | AF3 |
Number of Residues | 7 |
Details | binding site for residue EPE G 503 |
Chain | Residue |
G | SER357 |
G | ARG379 |
G | HOH662 |
H | TYR356 |
H | SER357 |
H | ARG379 |
H | HOH746 |
site_id | AF4 |
Number of Residues | 6 |
Details | binding site for residue MG G 504 |
Chain | Residue |
G | ALA276 |
G | ALA279 |
G | GLN308 |
G | HOH606 |
G | HOH895 |
G | HOH906 |
site_id | AF5 |
Number of Residues | 3 |
Details | binding site for residue PEG G 505 |
Chain | Residue |
G | GLU64 |
G | TRP65 |
G | LYS334 |
site_id | AF6 |
Number of Residues | 5 |
Details | binding site for residue MG G 506 |
Chain | Residue |
E | HOH907 |
G | HOH739 |
H | HOH643 |
H | HOH895 |
H | HOH911 |
site_id | AF7 |
Number of Residues | 5 |
Details | binding site for residue MG H 501 |
Chain | Residue |
E | HOH910 |
H | ASP34 |
H | HOH624 |
H | HOH736 |
H | HOH762 |
site_id | AF8 |
Number of Residues | 14 |
Details | binding site for residue PYR H 502 |
Chain | Residue |
H | TYR89 |
H | SER91 |
H | GLY92 |
H | TRP93 |
H | ASP153 |
H | HIS180 |
H | EJA191 |
H | ARG228 |
H | TRP283 |
H | THR347 |
H | MG503 |
H | HOH605 |
H | HOH648 |
H | HOH652 |
site_id | AF9 |
Number of Residues | 5 |
Details | binding site for residue MG H 503 |
Chain | Residue |
H | ASP153 |
H | PYR502 |
H | HOH605 |
H | HOH648 |
H | HOH652 |
site_id | AG1 |
Number of Residues | 6 |
Details | binding site for residue MG H 504 |
Chain | Residue |
F | HOH965 |
G | HOH953 |
H | HOH640 |
H | HOH696 |
H | HOH698 |
H | HOH856 |
site_id | AG2 |
Number of Residues | 6 |
Details | binding site for residue MG H 505 |
Chain | Residue |
H | ALA276 |
H | ALA279 |
H | GLN308 |
H | HOH645 |
H | HOH877 |
H | HOH896 |
site_id | AG3 |
Number of Residues | 4 |
Details | binding site for residue PEG H 506 |
Chain | Residue |
H | TRP65 |
H | ASN67 |
H | HOH777 |
H | HOH843 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:24354272 |
Chain | Residue | Details |
A | EJA191 | |
B | EJA191 | |
C | EJA191 | |
D | EJA191 | |
E | EJA191 | |
F | EJA191 | |
G | EJA191 | |
H | EJA191 |
site_id | SWS_FT_FI2 |
Number of Residues | 48 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10932251 |
Chain | Residue | Details |
A | SER91 | |
B | ARG228 | |
B | ASN313 | |
B | THR347 | |
C | SER91 | |
C | ASP153 | |
C | GLY192 | |
C | ARG228 | |
C | ASN313 | |
C | THR347 | |
D | SER91 | |
A | ASP153 | |
D | ASP153 | |
D | GLY192 | |
D | ARG228 | |
D | ASN313 | |
D | THR347 | |
E | SER91 | |
E | ASP153 | |
E | GLY192 | |
E | ARG228 | |
E | ASN313 | |
A | GLY192 | |
E | THR347 | |
F | SER91 | |
F | ASP153 | |
F | GLY192 | |
F | ARG228 | |
F | ASN313 | |
F | THR347 | |
G | SER91 | |
G | ASP153 | |
G | GLY192 | |
A | ARG228 | |
G | ARG228 | |
G | ASN313 | |
G | THR347 | |
H | SER91 | |
H | ASP153 | |
H | GLY192 | |
H | ARG228 | |
H | ASN313 | |
H | THR347 | |
A | ASN313 | |
A | THR347 | |
B | SER91 | |
B | ASP153 | |
B | GLY192 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | CROSSLNK: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup) => ECO:0000269|PubMed:20066036 |
Chain | Residue | Details |
A | LYS334 | |
F | LYS334 | |
G | LYS334 | |
H | LYS334 | |
B | LYS334 | |
C | LYS334 | |
D | LYS334 | |
E | LYS334 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 272 |
Chain | Residue | Details |
A | ASP153 | metal ligand |
A | HIS180 | electrostatic stabiliser, hydrogen bond donor |
A | EJA191 | covalent catalysis, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, proton shuttle (general acid/base) |
A | HIS193 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton shuttle (general acid/base) |
A | ARG228 | electrostatic stabiliser, hydrogen bond donor |
A | SER315 | electrostatic stabiliser, hydrogen bond donor |
A | SER317 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 7 |
Details | M-CSA 272 |
Chain | Residue | Details |
B | ASP153 | metal ligand |
B | HIS180 | electrostatic stabiliser, hydrogen bond donor |
B | EJA191 | covalent catalysis, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, proton shuttle (general acid/base) |
B | HIS193 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton shuttle (general acid/base) |
B | ARG228 | electrostatic stabiliser, hydrogen bond donor |
B | SER315 | electrostatic stabiliser, hydrogen bond donor |
B | SER317 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA3 |
Number of Residues | 7 |
Details | M-CSA 272 |
Chain | Residue | Details |
C | ASP153 | metal ligand |
C | HIS180 | electrostatic stabiliser, hydrogen bond donor |
C | EJA191 | covalent catalysis, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, proton shuttle (general acid/base) |
C | HIS193 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton shuttle (general acid/base) |
C | ARG228 | electrostatic stabiliser, hydrogen bond donor |
C | SER315 | electrostatic stabiliser, hydrogen bond donor |
C | SER317 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA4 |
Number of Residues | 7 |
Details | M-CSA 272 |
Chain | Residue | Details |
D | ASP153 | metal ligand |
D | HIS180 | electrostatic stabiliser, hydrogen bond donor |
D | EJA191 | covalent catalysis, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, proton shuttle (general acid/base) |
D | HIS193 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton shuttle (general acid/base) |
D | ARG228 | electrostatic stabiliser, hydrogen bond donor |
D | SER315 | electrostatic stabiliser, hydrogen bond donor |
D | SER317 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA5 |
Number of Residues | 7 |
Details | M-CSA 272 |
Chain | Residue | Details |
E | ASP153 | metal ligand |
E | HIS180 | electrostatic stabiliser, hydrogen bond donor |
E | EJA191 | covalent catalysis, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, proton shuttle (general acid/base) |
E | HIS193 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton shuttle (general acid/base) |
E | ARG228 | electrostatic stabiliser, hydrogen bond donor |
E | SER315 | electrostatic stabiliser, hydrogen bond donor |
E | SER317 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA6 |
Number of Residues | 7 |
Details | M-CSA 272 |
Chain | Residue | Details |
F | ASP153 | metal ligand |
F | HIS180 | electrostatic stabiliser, hydrogen bond donor |
F | EJA191 | covalent catalysis, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, proton shuttle (general acid/base) |
F | HIS193 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton shuttle (general acid/base) |
F | ARG228 | electrostatic stabiliser, hydrogen bond donor |
F | SER315 | electrostatic stabiliser, hydrogen bond donor |
F | SER317 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA7 |
Number of Residues | 7 |
Details | M-CSA 272 |
Chain | Residue | Details |
G | ASP153 | metal ligand |
G | HIS180 | electrostatic stabiliser, hydrogen bond donor |
G | EJA191 | covalent catalysis, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, proton shuttle (general acid/base) |
G | HIS193 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton shuttle (general acid/base) |
G | ARG228 | electrostatic stabiliser, hydrogen bond donor |
G | SER315 | electrostatic stabiliser, hydrogen bond donor |
G | SER317 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA8 |
Number of Residues | 7 |
Details | M-CSA 272 |
Chain | Residue | Details |
H | ASP153 | metal ligand |
H | HIS180 | electrostatic stabiliser, hydrogen bond donor |
H | EJA191 | covalent catalysis, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, proton shuttle (general acid/base) |
H | HIS193 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton shuttle (general acid/base) |
H | ARG228 | electrostatic stabiliser, hydrogen bond donor |
H | SER315 | electrostatic stabiliser, hydrogen bond donor |
H | SER317 | electrostatic stabiliser, hydrogen bond donor |