4QII
Crystal Structure of type II MenB from Mycobacteria tuberculosis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005886 | cellular_component | plasma membrane |
A | 0008935 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA synthase activity |
A | 0009234 | biological_process | menaquinone biosynthetic process |
A | 0016829 | molecular_function | lyase activity |
A | 0034214 | biological_process | protein hexamerization |
B | 0005886 | cellular_component | plasma membrane |
B | 0008935 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA synthase activity |
B | 0009234 | biological_process | menaquinone biosynthetic process |
B | 0016829 | molecular_function | lyase activity |
B | 0034214 | biological_process | protein hexamerization |
C | 0005886 | cellular_component | plasma membrane |
C | 0008935 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA synthase activity |
C | 0009234 | biological_process | menaquinone biosynthetic process |
C | 0016829 | molecular_function | lyase activity |
C | 0034214 | biological_process | protein hexamerization |
D | 0005886 | cellular_component | plasma membrane |
D | 0008935 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA synthase activity |
D | 0009234 | biological_process | menaquinone biosynthetic process |
D | 0016829 | molecular_function | lyase activity |
D | 0034214 | biological_process | protein hexamerization |
E | 0005886 | cellular_component | plasma membrane |
E | 0008935 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA synthase activity |
E | 0009234 | biological_process | menaquinone biosynthetic process |
E | 0016829 | molecular_function | lyase activity |
E | 0034214 | biological_process | protein hexamerization |
F | 0005886 | cellular_component | plasma membrane |
F | 0008935 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA synthase activity |
F | 0009234 | biological_process | menaquinone biosynthetic process |
F | 0016829 | molecular_function | lyase activity |
F | 0034214 | biological_process | protein hexamerization |
G | 0005886 | cellular_component | plasma membrane |
G | 0008935 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA synthase activity |
G | 0009234 | biological_process | menaquinone biosynthetic process |
G | 0016829 | molecular_function | lyase activity |
G | 0034214 | biological_process | protein hexamerization |
H | 0005886 | cellular_component | plasma membrane |
H | 0008935 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA synthase activity |
H | 0009234 | biological_process | menaquinone biosynthetic process |
H | 0016829 | molecular_function | lyase activity |
H | 0034214 | biological_process | protein hexamerization |
I | 0005886 | cellular_component | plasma membrane |
I | 0008935 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA synthase activity |
I | 0009234 | biological_process | menaquinone biosynthetic process |
I | 0016829 | molecular_function | lyase activity |
I | 0034214 | biological_process | protein hexamerization |
J | 0005886 | cellular_component | plasma membrane |
J | 0008935 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA synthase activity |
J | 0009234 | biological_process | menaquinone biosynthetic process |
J | 0016829 | molecular_function | lyase activity |
J | 0034214 | biological_process | protein hexamerization |
K | 0005886 | cellular_component | plasma membrane |
K | 0008935 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA synthase activity |
K | 0009234 | biological_process | menaquinone biosynthetic process |
K | 0016829 | molecular_function | lyase activity |
K | 0034214 | biological_process | protein hexamerization |
L | 0005886 | cellular_component | plasma membrane |
L | 0008935 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA synthase activity |
L | 0009234 | biological_process | menaquinone biosynthetic process |
L | 0016829 | molecular_function | lyase activity |
L | 0034214 | biological_process | protein hexamerization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE 2NE A 401 |
Chain | Residue |
A | VAL57 |
A | ILE136 |
A | TRP157 |
A | GLY160 |
A | GLY161 |
A | THR184 |
A | ASP185 |
A | VAL188 |
A | SER190 |
A | HOH597 |
A | HOH600 |
A | ARG58 |
A | HOH709 |
A | HOH737 |
F | PHE299 |
F | LYS302 |
F | HOH577 |
G | ALA14 |
G | LEU15 |
A | ALA60 |
A | PHE61 |
A | SER103 |
A | GLY104 |
A | GLY105 |
A | ASP106 |
A | GLN107 |
site_id | AC2 |
Number of Residues | 35 |
Details | BINDING SITE FOR RESIDUE 2NE B 401 |
Chain | Residue |
B | GLU56 |
B | VAL57 |
B | ARG58 |
B | ALA60 |
B | LYS95 |
B | SER103 |
B | GLY104 |
B | GLY105 |
B | ASP106 |
B | GLN107 |
B | TYR115 |
B | TRP157 |
B | GLY161 |
B | THR184 |
B | ASP185 |
B | VAL188 |
B | SER190 |
B | HOH542 |
B | HOH601 |
B | HOH608 |
B | HOH627 |
B | HOH637 |
B | HOH638 |
B | HOH648 |
B | HOH692 |
B | HOH699 |
B | HOH707 |
B | HOH737 |
B | HOH789 |
B | HOH817 |
E | PHE299 |
E | LYS302 |
E | HOH533 |
I | ALA14 |
I | LEU15 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PGE B 402 |
Chain | Residue |
A | VAL204 |
B | ARG202 |
B | MET227 |
B | HOH683 |
C | GLN203 |
site_id | AC4 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE 2NE C 401 |
Chain | Residue |
C | VAL57 |
C | ARG58 |
C | ALA60 |
C | SER103 |
C | GLY104 |
C | GLY105 |
C | ASP106 |
C | GLN107 |
C | TRP157 |
C | GLY160 |
C | GLY161 |
C | THR184 |
C | ASP185 |
C | SER190 |
C | HOH547 |
C | HOH625 |
C | HOH632 |
C | HOH643 |
C | HOH648 |
C | HOH652 |
C | HOH679 |
C | HOH683 |
C | HOH749 |
C | HOH819 |
D | PHE299 |
D | LYS302 |
D | HOH651 |
H | ALA14 |
H | LEU15 |
site_id | AC5 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE 2NE D 401 |
Chain | Residue |
D | GLU56 |
D | VAL57 |
D | ARG58 |
D | ALA60 |
D | SER103 |
D | GLY104 |
D | GLY105 |
D | ASP106 |
D | GLN107 |
D | TYR115 |
D | TRP157 |
D | GLY161 |
D | THR184 |
D | ASP185 |
D | SER190 |
D | HOH614 |
D | HOH619 |
D | HOH647 |
D | HOH667 |
D | HOH697 |
A | SER119 |
C | TYR287 |
C | PHE299 |
C | LYS302 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PGE D 402 |
Chain | Residue |
D | ARG202 |
D | GLN203 |
D | MET227 |
D | HOH515 |
D | HOH718 |
E | MET227 |
site_id | AC7 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE 2NE E 401 |
Chain | Residue |
B | TYR287 |
B | PHE299 |
B | LYS302 |
B | HOH571 |
E | GLU56 |
E | VAL57 |
E | ARG58 |
E | ALA60 |
E | LYS95 |
E | SER103 |
E | GLY104 |
E | GLY105 |
E | ASP106 |
E | GLN107 |
E | TYR115 |
E | TRP157 |
E | GLY161 |
E | THR184 |
E | ASP185 |
E | VAL188 |
E | SER190 |
E | HOH530 |
E | HOH542 |
E | HOH621 |
E | HOH635 |
E | HOH703 |
E | HOH708 |
E | HOH709 |
E | HOH717 |
E | HOH740 |
E | HOH795 |
E | HOH808 |
E | HOH813 |
E | HOH819 |
site_id | AC8 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE 2NE F 401 |
Chain | Residue |
A | TYR287 |
A | PHE299 |
A | LYS302 |
A | HOH678 |
F | GLU56 |
F | VAL57 |
F | ARG58 |
F | ALA60 |
F | LYS95 |
F | SER103 |
F | GLY104 |
F | GLY105 |
F | ASP106 |
F | GLN107 |
F | TYR115 |
F | TRP157 |
F | GLY161 |
F | THR184 |
F | ASP185 |
F | VAL188 |
F | SER190 |
F | HOH561 |
F | HOH563 |
F | HOH584 |
F | HOH617 |
F | HOH680 |
F | HOH723 |
F | HOH727 |
F | HOH751 |
F | HOH784 |
F | HOH796 |
site_id | AC9 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE 2NE G 401 |
Chain | Residue |
A | LEU15 |
G | VAL57 |
G | ARG58 |
G | ALA60 |
G | LYS95 |
G | SER103 |
G | GLY104 |
G | GLY105 |
G | ASP106 |
G | GLN107 |
G | TYR115 |
G | TRP157 |
G | GLY161 |
G | THR184 |
G | ASP185 |
G | SER190 |
G | HOH536 |
G | HOH588 |
G | HOH599 |
G | HOH610 |
G | HOH635 |
G | HOH636 |
G | HOH656 |
G | HOH680 |
G | HOH707 |
G | HOH721 |
G | HOH726 |
L | PHE299 |
L | LYS302 |
L | HOH588 |
L | HOH774 |
site_id | BC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PGE G 402 |
Chain | Residue |
G | ALA201 |
G | ARG202 |
G | GLN203 |
G | MET227 |
G | HOH629 |
H | HOH758 |
I | ARG202 |
I | VAL204 |
I | MET227 |
site_id | BC2 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE 2NE H 401 |
Chain | Residue |
C | ALA14 |
C | LEU15 |
H | VAL57 |
H | ARG58 |
H | ALA60 |
H | LYS95 |
H | SER103 |
H | GLY104 |
H | GLY105 |
H | ASP106 |
H | GLN107 |
H | TYR115 |
H | LEU134 |
H | TRP157 |
H | GLY161 |
H | THR184 |
H | ASP185 |
H | SER190 |
H | HOH512 |
H | HOH540 |
H | HOH588 |
H | HOH633 |
H | HOH647 |
H | HOH665 |
H | HOH669 |
H | HOH692 |
H | HOH714 |
H | HOH751 |
H | HOH774 |
K | TYR287 |
K | PHE299 |
K | LYS302 |
K | HOH582 |
K | HOH721 |
site_id | BC3 |
Number of Residues | 35 |
Details | BINDING SITE FOR RESIDUE 2NE I 401 |
Chain | Residue |
B | ALA14 |
B | LEU15 |
I | VAL57 |
I | ARG58 |
I | ALA60 |
I | LYS95 |
I | SER103 |
I | GLY104 |
I | GLY105 |
I | ASP106 |
I | GLN107 |
I | TYR115 |
I | LEU134 |
I | TRP157 |
I | GLY161 |
I | THR184 |
I | ASP185 |
I | VAL188 |
I | SER190 |
I | HOH544 |
I | HOH573 |
I | HOH579 |
I | HOH651 |
I | HOH660 |
I | HOH673 |
I | HOH678 |
I | HOH725 |
I | HOH732 |
I | HOH777 |
I | HOH826 |
J | TYR287 |
J | PHE299 |
J | LYS302 |
J | HOH575 |
J | HOH602 |
site_id | BC4 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE 2NE J 401 |
Chain | Residue |
I | PHE299 |
I | LYS302 |
I | HOH656 |
J | VAL57 |
J | ARG58 |
J | SER103 |
J | GLY104 |
J | GLY105 |
J | ASP106 |
J | GLN107 |
J | TYR115 |
J | TRP157 |
J | GLY161 |
J | THR184 |
J | ASP185 |
J | VAL188 |
J | SER190 |
J | HOH564 |
J | HOH627 |
J | HOH688 |
J | HOH692 |
J | HOH712 |
J | HOH720 |
J | HOH724 |
J | HOH743 |
J | HOH753 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PGE J 402 |
Chain | Residue |
J | ARG202 |
J | HOH542 |
J | HOH623 |
J | HOH674 |
K | ARG202 |
L | ARG202 |
site_id | BC6 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE 2NE K 401 |
Chain | Residue |
H | TYR287 |
H | PHE299 |
H | LYS302 |
H | HOH656 |
K | GLU56 |
K | VAL57 |
K | ARG58 |
K | ALA60 |
K | LYS95 |
K | SER103 |
K | GLY104 |
K | GLY105 |
K | ASP106 |
K | GLN107 |
K | TYR115 |
K | TRP157 |
K | GLY161 |
K | THR184 |
K | ASP185 |
K | VAL188 |
K | SER190 |
K | HOH572 |
K | HOH608 |
K | HOH621 |
K | HOH674 |
K | HOH675 |
K | HOH725 |
K | HOH741 |
site_id | BC7 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE 2NE L 401 |
Chain | Residue |
G | TYR287 |
G | PHE299 |
G | LYS302 |
G | HOH683 |
L | GLU56 |
L | VAL57 |
L | ARG58 |
L | ALA60 |
L | LYS95 |
L | SER103 |
L | GLY104 |
L | GLY105 |
L | ASP106 |
L | GLN107 |
L | TYR115 |
L | TRP157 |
L | GLY161 |
L | THR184 |
L | ASP185 |
L | SER190 |
L | HOH572 |
L | HOH623 |
L | HOH636 |
L | HOH706 |
L | HOH778 |
L | HOH783 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_01934, ECO:0000269|PubMed:12909628, ECO:0000269|PubMed:21830810 |
Chain | Residue | Details |
A | ARG58 | |
J | ARG58 | |
K | ARG58 | |
L | ARG58 | |
B | ARG58 | |
C | ARG58 | |
D | ARG58 | |
E | ARG58 | |
F | ARG58 | |
G | ARG58 | |
H | ARG58 | |
I | ARG58 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: in other chain => ECO:0000269|PubMed:12909628, ECO:0000269|PubMed:21830810 |
Chain | Residue | Details |
A | LYS95 | |
J | LYS95 | |
K | LYS95 | |
L | LYS95 | |
B | LYS95 | |
C | LYS95 | |
D | LYS95 | |
E | LYS95 | |
F | LYS95 | |
G | LYS95 | |
H | LYS95 | |
I | LYS95 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_01934, ECO:0000269|PubMed:12909628, ECO:0000269|PubMed:16131752, ECO:0000269|PubMed:21830810 |
Chain | Residue | Details |
A | SER103 | |
J | SER103 | |
K | SER103 | |
L | SER103 | |
B | SER103 | |
C | SER103 | |
D | SER103 | |
E | SER103 | |
F | SER103 | |
G | SER103 | |
H | SER103 | |
I | SER103 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | BINDING: in other chain => ECO:0000250|UniProtKB:P0ABU0, ECO:0000255|HAMAP-Rule:MF_01934 |
Chain | Residue | Details |
A | TYR115 | |
J | TYR115 | |
K | TYR115 | |
L | TYR115 | |
B | TYR115 | |
C | TYR115 | |
D | TYR115 | |
E | TYR115 | |
F | TYR115 | |
G | TYR115 | |
H | TYR115 | |
I | TYR115 |
site_id | SWS_FT_FI5 |
Number of Residues | 24 |
Details | BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_01934, ECO:0000269|PubMed:12909628 |
Chain | Residue | Details |
A | TRP157 | |
E | THR184 | |
F | TRP157 | |
F | THR184 | |
G | TRP157 | |
G | THR184 | |
H | TRP157 | |
H | THR184 | |
I | TRP157 | |
I | THR184 | |
J | TRP157 | |
A | THR184 | |
J | THR184 | |
K | TRP157 | |
K | THR184 | |
L | TRP157 | |
L | THR184 | |
B | TRP157 | |
B | THR184 | |
C | TRP157 | |
C | THR184 | |
D | TRP157 | |
D | THR184 | |
E | TRP157 |
site_id | SWS_FT_FI6 |
Number of Residues | 12 |
Details | BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_01934, ECO:0000305|PubMed:21830810 |
Chain | Residue | Details |
A | SER190 | |
J | SER190 | |
K | SER190 | |
L | SER190 | |
B | SER190 | |
C | SER190 | |
D | SER190 | |
E | SER190 | |
F | SER190 | |
G | SER190 | |
H | SER190 | |
I | SER190 |
site_id | SWS_FT_FI7 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P0ABU0, ECO:0000255|HAMAP-Rule:MF_01934 |
Chain | Residue | Details |
A | TYR287 | |
E | LYS302 | |
F | TYR287 | |
F | LYS302 | |
G | TYR287 | |
G | LYS302 | |
H | TYR287 | |
H | LYS302 | |
I | TYR287 | |
I | LYS302 | |
J | TYR287 | |
A | LYS302 | |
J | LYS302 | |
K | TYR287 | |
K | LYS302 | |
L | TYR287 | |
L | LYS302 | |
B | TYR287 | |
B | LYS302 | |
C | TYR287 | |
C | LYS302 | |
D | TYR287 | |
D | LYS302 | |
E | TYR287 |
site_id | SWS_FT_FI8 |
Number of Residues | 12 |
Details | SITE: Important for catalysis => ECO:0000250|UniProtKB:P0ABU0, ECO:0000255|HAMAP-Rule:MF_01934 |
Chain | Residue | Details |
A | TYR115 | |
J | TYR115 | |
K | TYR115 | |
L | TYR115 | |
B | TYR115 | |
C | TYR115 | |
D | TYR115 | |
E | TYR115 | |
F | TYR115 | |
G | TYR115 | |
H | TYR115 | |
I | TYR115 |
site_id | SWS_FT_FI9 |
Number of Residues | 12 |
Details | SITE: Important for catalysis => ECO:0000255|HAMAP-Rule:MF_01934, ECO:0000305|PubMed:20643650, ECO:0000305|PubMed:21830810 |
Chain | Residue | Details |
A | ASP185 | |
J | ASP185 | |
K | ASP185 | |
L | ASP185 | |
B | ASP185 | |
C | ASP185 | |
D | ASP185 | |
E | ASP185 | |
F | ASP185 | |
G | ASP185 | |
H | ASP185 | |
I | ASP185 |
site_id | SWS_FT_FI10 |
Number of Residues | 12 |
Details | SITE: Important for catalysis => ECO:0000250|UniProtKB:P0ABU0, ECO:0000255|HAMAP-Rule:MF_01934, ECO:0000305|PubMed:12909628 |
Chain | Residue | Details |
A | TYR287 | |
J | TYR287 | |
K | TYR287 | |
L | TYR287 | |
B | TYR287 | |
C | TYR287 | |
D | TYR287 | |
E | TYR287 | |
F | TYR287 | |
G | TYR287 | |
H | TYR287 | |
I | TYR287 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 346 |
Chain | Residue | Details |
A | GLY105 | electrostatic stabiliser, hydrogen bond donor |
A | TYR115 | electrostatic stabiliser, hydrogen bond donor, steric role |
A | GLY161 | electrostatic stabiliser, hydrogen bond donor |
A | ASP185 | activator |
A | SER190 | activator |
A | TYR287 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, steric role |
site_id | MCSA10 |
Number of Residues | 6 |
Details | M-CSA 346 |
Chain | Residue | Details |
J | GLY105 | electrostatic stabiliser, hydrogen bond donor |
J | TYR115 | electrostatic stabiliser, hydrogen bond donor, steric role |
J | GLY161 | electrostatic stabiliser, hydrogen bond donor |
J | ASP185 | activator |
J | SER190 | activator |
J | TYR287 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, steric role |
site_id | MCSA11 |
Number of Residues | 6 |
Details | M-CSA 346 |
Chain | Residue | Details |
K | GLY105 | electrostatic stabiliser, hydrogen bond donor |
K | TYR115 | electrostatic stabiliser, hydrogen bond donor, steric role |
K | GLY161 | electrostatic stabiliser, hydrogen bond donor |
K | ASP185 | activator |
K | SER190 | activator |
K | TYR287 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, steric role |
site_id | MCSA12 |
Number of Residues | 6 |
Details | M-CSA 346 |
Chain | Residue | Details |
L | GLY105 | electrostatic stabiliser, hydrogen bond donor |
L | TYR115 | electrostatic stabiliser, hydrogen bond donor, steric role |
L | GLY161 | electrostatic stabiliser, hydrogen bond donor |
L | ASP185 | activator |
L | SER190 | activator |
L | TYR287 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, steric role |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 346 |
Chain | Residue | Details |
B | GLY105 | electrostatic stabiliser, hydrogen bond donor |
B | TYR115 | electrostatic stabiliser, hydrogen bond donor, steric role |
B | GLY161 | electrostatic stabiliser, hydrogen bond donor |
B | ASP185 | activator |
B | SER190 | activator |
B | TYR287 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, steric role |
site_id | MCSA3 |
Number of Residues | 6 |
Details | M-CSA 346 |
Chain | Residue | Details |
C | GLY105 | electrostatic stabiliser, hydrogen bond donor |
C | TYR115 | electrostatic stabiliser, hydrogen bond donor, steric role |
C | GLY161 | electrostatic stabiliser, hydrogen bond donor |
C | ASP185 | activator |
C | SER190 | activator |
C | TYR287 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, steric role |
site_id | MCSA4 |
Number of Residues | 6 |
Details | M-CSA 346 |
Chain | Residue | Details |
D | GLY105 | electrostatic stabiliser, hydrogen bond donor |
D | TYR115 | electrostatic stabiliser, hydrogen bond donor, steric role |
D | GLY161 | electrostatic stabiliser, hydrogen bond donor |
D | ASP185 | activator |
D | SER190 | activator |
D | TYR287 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, steric role |
site_id | MCSA5 |
Number of Residues | 6 |
Details | M-CSA 346 |
Chain | Residue | Details |
E | GLY105 | electrostatic stabiliser, hydrogen bond donor |
E | TYR115 | electrostatic stabiliser, hydrogen bond donor, steric role |
E | GLY161 | electrostatic stabiliser, hydrogen bond donor |
E | ASP185 | activator |
E | SER190 | activator |
E | TYR287 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, steric role |
site_id | MCSA6 |
Number of Residues | 6 |
Details | M-CSA 346 |
Chain | Residue | Details |
F | GLY105 | electrostatic stabiliser, hydrogen bond donor |
F | TYR115 | electrostatic stabiliser, hydrogen bond donor, steric role |
F | GLY161 | electrostatic stabiliser, hydrogen bond donor |
F | ASP185 | activator |
F | SER190 | activator |
F | TYR287 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, steric role |
site_id | MCSA7 |
Number of Residues | 6 |
Details | M-CSA 346 |
Chain | Residue | Details |
G | GLY105 | electrostatic stabiliser, hydrogen bond donor |
G | TYR115 | electrostatic stabiliser, hydrogen bond donor, steric role |
G | GLY161 | electrostatic stabiliser, hydrogen bond donor |
G | ASP185 | activator |
G | SER190 | activator |
G | TYR287 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, steric role |
site_id | MCSA8 |
Number of Residues | 6 |
Details | M-CSA 346 |
Chain | Residue | Details |
H | GLY105 | electrostatic stabiliser, hydrogen bond donor |
H | TYR115 | electrostatic stabiliser, hydrogen bond donor, steric role |
H | GLY161 | electrostatic stabiliser, hydrogen bond donor |
H | ASP185 | activator |
H | SER190 | activator |
H | TYR287 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, steric role |
site_id | MCSA9 |
Number of Residues | 6 |
Details | M-CSA 346 |
Chain | Residue | Details |
I | GLY105 | electrostatic stabiliser, hydrogen bond donor |
I | TYR115 | electrostatic stabiliser, hydrogen bond donor, steric role |
I | GLY161 | electrostatic stabiliser, hydrogen bond donor |
I | ASP185 | activator |
I | SER190 | activator |
I | TYR287 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, steric role |