4QIJ
Crystal structure of MenB from Mycobacteria tuberculosis in complex with 1-HNA-CoA
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 | 29 |
| Details | BINDING SITE FOR RESIDUE 1HA A 401 |
| Chain | Residue |
| A | GLU56 |
| A | ASP106 |
| A | GLN107 |
| A | TYR115 |
| A | LEU134 |
| A | ILE136 |
| A | TRP157 |
| A | GLY161 |
| A | THR184 |
| A | ASP185 |
| A | SER190 |
| A | VAL57 |
| A | HOH602 |
| A | HOH605 |
| A | HOH617 |
| A | HOH685 |
| F | PHE299 |
| F | LYS302 |
| F | HOH649 |
| L | ALA14 |
| L | LEU15 |
| L | HOH576 |
| A | ARG58 |
| A | ALA60 |
| A | PHE61 |
| A | LYS95 |
| A | SER103 |
| A | GLY104 |
| A | GLY105 |
| site_id | AC2 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE 1HA 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 | ILE136 |
| B | LEU137 |
| B | TRP157 |
| B | GLY161 |
| B | THR184 |
| B | ASP185 |
| B | SER190 |
| B | PHE191 |
| B | HOH518 |
| B | HOH551 |
| B | HOH567 |
| B | HOH578 |
| B | HOH591 |
| B | HOH608 |
| B | HOH655 |
| B | HOH688 |
| B | HOH694 |
| B | HOH707 |
| E | PHE299 |
| E | LYS302 |
| K | ALA14 |
| K | LEU15 |
| site_id | AC3 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE 1HA C 401 |
| Chain | Residue |
| C | GLU56 |
| C | VAL57 |
| C | ARG58 |
| C | ALA60 |
| C | LYS95 |
| C | SER103 |
| C | GLY104 |
| C | GLY105 |
| C | ASP106 |
| C | GLN107 |
| C | TYR115 |
| C | ILE136 |
| C | LEU137 |
| C | TRP157 |
| C | GLY161 |
| C | THR184 |
| C | ASP185 |
| C | SER190 |
| C | PHE191 |
| C | HOH525 |
| C | HOH532 |
| C | HOH579 |
| C | HOH584 |
| C | HOH585 |
| C | HOH623 |
| C | HOH625 |
| C | HOH638 |
| C | HOH685 |
| D | PHE299 |
| D | LYS302 |
| J | ALA14 |
| J | LEU15 |
| site_id | AC4 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE 1HA D 401 |
| Chain | Residue |
| D | ALA60 |
| D | LYS95 |
| D | SER103 |
| D | GLY104 |
| D | GLY105 |
| D | ASP106 |
| D | GLN107 |
| D | TYR115 |
| D | ILE136 |
| D | TRP157 |
| D | GLY161 |
| D | THR184 |
| D | ASP185 |
| D | SER190 |
| D | PHE191 |
| D | HOH604 |
| D | HOH618 |
| D | HOH628 |
| D | HOH649 |
| I | HOH585 |
| I | HOH616 |
| I | HOH701 |
| C | PHE299 |
| C | LYS302 |
| C | HOH630 |
| D | VAL57 |
| D | ARG58 |
| site_id | AC5 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE 1HA E 401 |
| Chain | Residue |
| B | PHE299 |
| B | LYS302 |
| E | GLU56 |
| E | VAL57 |
| E | ARG58 |
| E | ALA60 |
| E | LYS95 |
| E | SER103 |
| E | GLY104 |
| E | GLY105 |
| E | ASP106 |
| E | GLN107 |
| E | ILE136 |
| E | LEU137 |
| E | TRP157 |
| E | GLY160 |
| E | GLY161 |
| E | THR184 |
| E | ASP185 |
| E | VAL188 |
| E | SER190 |
| E | PHE191 |
| E | ASP192 |
| E | HOH562 |
| E | HOH568 |
| E | HOH576 |
| E | HOH611 |
| site_id | AC6 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE 1HA F 401 |
| Chain | Residue |
| A | PHE299 |
| A | LYS302 |
| F | GLU56 |
| F | VAL57 |
| F | ARG58 |
| F | ALA60 |
| F | LYS95 |
| F | SER103 |
| F | GLY104 |
| F | GLY105 |
| F | ASP106 |
| F | GLN107 |
| F | TYR115 |
| F | ILE136 |
| F | LEU137 |
| F | TRP157 |
| F | GLY161 |
| F | THR184 |
| F | ASP185 |
| F | VAL188 |
| F | SER190 |
| F | PHE191 |
| F | HOH512 |
| F | HOH517 |
| F | HOH539 |
| F | HOH550 |
| F | HOH553 |
| F | HOH612 |
| site_id | AC7 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE 1HA G 401 |
| Chain | Residue |
| G | GLU56 |
| G | VAL57 |
| G | ARG58 |
| G | ALA60 |
| G | LYS95 |
| G | SER103 |
| G | GLY104 |
| G | GLY105 |
| G | ASP106 |
| G | GLN107 |
| G | TYR115 |
| G | LEU137 |
| G | TRP157 |
| G | GLY161 |
| G | THR184 |
| G | ASP185 |
| G | VAL188 |
| G | SER190 |
| G | PHE191 |
| G | HOH537 |
| G | HOH594 |
| K | PHE299 |
| K | LYS302 |
| L | SER119 |
| site_id | AC8 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE 1HA H 401 |
| Chain | Residue |
| H | GLU56 |
| H | VAL57 |
| H | ARG58 |
| H | ALA60 |
| H | LYS95 |
| H | SER103 |
| H | GLY104 |
| H | GLY105 |
| H | ASP106 |
| H | GLN107 |
| H | TYR115 |
| H | ILE136 |
| H | LEU137 |
| H | TRP157 |
| H | GLY161 |
| H | THR184 |
| H | ASP185 |
| H | VAL188 |
| H | SER190 |
| H | PHE191 |
| H | HOH547 |
| H | HOH623 |
| H | HOH631 |
| H | HOH642 |
| J | PHE299 |
| J | LYS302 |
| J | HOH580 |
| site_id | AC9 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE 1HA I 401 |
| Chain | Residue |
| I | GLU56 |
| I | VAL57 |
| I | ARG58 |
| I | ALA60 |
| I | LYS95 |
| I | SER103 |
| I | GLY104 |
| I | GLY105 |
| I | ASP106 |
| I | GLN107 |
| I | TYR115 |
| I | ILE136 |
| I | LEU137 |
| I | TRP157 |
| I | GLY160 |
| I | GLY161 |
| I | THR184 |
| I | ASP185 |
| I | VAL188 |
| I | SER190 |
| I | PHE191 |
| I | HOH526 |
| I | HOH558 |
| I | HOH569 |
| I | HOH584 |
| I | HOH599 |
| I | HOH601 |
| I | HOH614 |
| I | HOH655 |
| I | HOH666 |
| I | HOH679 |
| I | HOH681 |
| L | PHE299 |
| L | LYS302 |
| site_id | BC1 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE 1HA J 401 |
| Chain | Residue |
| C | ALA14 |
| C | LEU15 |
| H | PHE299 |
| H | LYS302 |
| J | GLU56 |
| J | VAL57 |
| J | ARG58 |
| J | ALA60 |
| J | LYS95 |
| J | SER103 |
| J | GLY104 |
| J | GLY105 |
| J | ASP106 |
| J | GLN107 |
| J | TYR115 |
| J | ILE136 |
| J | TRP157 |
| J | GLY161 |
| J | THR184 |
| J | ASP185 |
| J | VAL188 |
| J | SER190 |
| J | PHE191 |
| J | HOH514 |
| J | HOH545 |
| J | HOH554 |
| J | HOH557 |
| J | HOH594 |
| J | HOH612 |
| J | HOH672 |
| J | HOH722 |
| site_id | BC2 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE 1HA K 401 |
| Chain | Residue |
| B | ALA14 |
| B | LEU15 |
| G | PHE299 |
| G | LYS302 |
| G | HOH584 |
| K | GLU56 |
| K | VAL57 |
| K | ARG58 |
| K | ALA60 |
| K | LYS95 |
| K | SER103 |
| K | GLY104 |
| K | GLY105 |
| K | ASP106 |
| K | GLN107 |
| K | TYR115 |
| K | ILE136 |
| K | LEU137 |
| K | TRP157 |
| K | GLY160 |
| K | GLY161 |
| K | THR184 |
| K | ASP185 |
| K | SER190 |
| K | PHE191 |
| K | HOH521 |
| K | HOH524 |
| K | HOH559 |
| K | HOH580 |
| K | HOH589 |
| K | HOH665 |
| K | HOH673 |
| K | HOH695 |
| site_id | BC3 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE 1HA L 401 |
| Chain | Residue |
| A | ALA14 |
| A | LEU15 |
| I | PHE299 |
| I | LYS302 |
| I | HOH595 |
| L | VAL57 |
| L | ARG58 |
| L | ALA60 |
| L | SER103 |
| L | GLY104 |
| L | GLY105 |
| L | ASP106 |
| L | GLN107 |
| L | TYR115 |
| L | TRP157 |
| L | GLY161 |
| L | THR184 |
| L | ASP185 |
| L | VAL188 |
| L | SER190 |
| L | PHE191 |
| L | HOH565 |
| L | HOH617 |
| L | HOH624 |
| L | HOH632 |
| L | HOH663 |
| L | HOH723 |
| L | HOH724 |
| L | HOH728 |
| L | HOH732 |
| L | HOH748 |
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 |
