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 |
| K | ARG58 | |
| L | ARG58 | |
| A | ARG58 | |
| B | ARG58 | |
| C | ARG58 | |
| D | ARG58 | |
| E | ARG58 | |
| F | ARG58 | |
| G | ARG58 | |
| H | ARG58 | |
| I | ARG58 | |
| J | 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 |
| D | LYS95 | |
| E | LYS95 | |
| F | LYS95 | |
| G | LYS95 | |
| H | LYS95 | |
| I | LYS95 | |
| J | LYS95 | |
| K | LYS95 | |
| L | LYS95 | |
| A | LYS95 | |
| B | LYS95 | |
| C | 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 |
| D | SER103 | |
| E | SER103 | |
| F | SER103 | |
| G | SER103 | |
| H | SER103 | |
| I | SER103 | |
| J | SER103 | |
| K | SER103 | |
| L | SER103 | |
| A | SER103 | |
| B | SER103 | |
| C | 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 | |
| B | TYR115 | |
| C | TYR115 | |
| D | TYR115 | |
| E | TYR115 | |
| F | TYR115 | |
| G | TYR115 | |
| H | TYR115 | |
| I | TYR115 | |
| J | TYR115 | |
| K | TYR115 | |
| L | 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 |
| G | TRP157 | |
| G | THR184 | |
| H | TRP157 | |
| H | THR184 | |
| I | TRP157 | |
| I | THR184 | |
| J | TRP157 | |
| J | THR184 | |
| K | TRP157 | |
| K | THR184 | |
| L | TRP157 | |
| L | THR184 | |
| A | TRP157 | |
| A | THR184 | |
| B | TRP157 | |
| B | THR184 | |
| C | TRP157 | |
| C | THR184 | |
| D | TRP157 | |
| D | THR184 | |
| E | TRP157 | |
| E | THR184 | |
| F | TRP157 | |
| F | THR184 |
| 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 | |
| B | SER190 | |
| C | SER190 | |
| D | SER190 | |
| E | SER190 | |
| F | SER190 | |
| G | SER190 | |
| H | SER190 | |
| I | SER190 | |
| J | SER190 | |
| K | SER190 | |
| L | 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 |
| G | TYR287 | |
| G | LYS302 | |
| H | TYR287 | |
| H | LYS302 | |
| I | TYR287 | |
| I | LYS302 | |
| J | TYR287 | |
| J | LYS302 | |
| K | TYR287 | |
| K | LYS302 | |
| L | TYR287 | |
| L | LYS302 | |
| A | TYR287 | |
| A | LYS302 | |
| B | TYR287 | |
| B | LYS302 | |
| C | TYR287 | |
| C | LYS302 | |
| D | TYR287 | |
| D | LYS302 | |
| E | TYR287 | |
| E | LYS302 | |
| F | TYR287 | |
| F | LYS302 |
| 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 | |
| B | TYR115 | |
| C | TYR115 | |
| D | TYR115 | |
| E | TYR115 | |
| F | TYR115 | |
| G | TYR115 | |
| H | TYR115 | |
| I | TYR115 | |
| J | TYR115 | |
| K | TYR115 | |
| L | 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 | |
| B | ASP185 | |
| C | ASP185 | |
| D | ASP185 | |
| E | ASP185 | |
| F | ASP185 | |
| G | ASP185 | |
| H | ASP185 | |
| I | ASP185 | |
| J | ASP185 | |
| K | ASP185 | |
| L | 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 | |
| B | TYR287 | |
| C | TYR287 | |
| D | TYR287 | |
| E | TYR287 | |
| F | TYR287 | |
| G | TYR287 | |
| H | TYR287 | |
| I | TYR287 | |
| J | TYR287 | |
| K | TYR287 | |
| L | 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 | 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 | 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 |
| F | GLY105 | electrostatic stabiliser, hydrogen bond donor |
| F | TYR115 | electrostatic stabiliser, hydrogen bond 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 |
| 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 | GLY161 | electrostatic stabiliser, hydrogen bond donor |
| K | SER190 | activator |
| K | TYR287 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, steric role |
| K | GLY105 | electrostatic stabiliser, hydrogen bond donor |
| K | TYR115 | electrostatic stabiliser, hydrogen bond donor, steric role |
| K | ASP185 | activator |
| 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 |
