6IYV
Crystal sturucture of L,D-transpeptidase LdtMt2 from Mycobacterium tuberculosis in complex with ertapenem adduct
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue 2RG B 501 |
| Chain | Residue |
| A | LYS299 |
| B | GOL506 |
| B | HOH622 |
| B | HOH624 |
| B | HOH693 |
| B | HOH742 |
| B | HOH757 |
| B | HOH774 |
| A | GLN363 |
| B | MET303 |
| B | TYR308 |
| B | VAL310 |
| B | TYR318 |
| B | GLY332 |
| B | HIS352 |
| B | CYS354 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue GOL B 502 |
| Chain | Residue |
| B | ASP251 |
| B | VAL253 |
| B | HIS368 |
| B | LYS370 |
| B | HOH601 |
| B | HOH628 |
| B | HOH734 |
| B | HOH767 |
| B | HOH854 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| B | GLU213 |
| B | HIS214 |
| B | PHE215 |
| B | ILE291 |
| B | HOH641 |
| B | HOH709 |
| B | HOH829 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| A | GLN400 |
| A | GOL503 |
| A | HOH639 |
| B | ASP251 |
| B | HOH618 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 505 |
| Chain | Residue |
| B | TYR366 |
| B | ASP367 |
| B | VAL369 |
| B | LYS370 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 506 |
| Chain | Residue |
| A | TRP324 |
| A | GLN363 |
| A | ASP367 |
| B | 2RG501 |
| B | HOH624 |
| B | HOH647 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | binding site for residue PEG B 507 |
| Chain | Residue |
| A | ARG181 |
| A | TRP202 |
| A | ASN204 |
| A | ASN405 |
| A | HOH702 |
| B | GLY161 |
| B | VAL222 |
| B | HIS246 |
| B | PHE247 |
| B | THR248 |
| B | HOH609 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue PEG B 508 |
| Chain | Residue |
| A | LYS407 |
| B | THR191 |
| B | THR192 |
| B | ASN193 |
| B | ASP223 |
| B | HOH605 |
| B | HOH747 |
| B | HOH779 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 B 509 |
| Chain | Residue |
| B | HOH603 |
| site_id | AD1 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| A | GLU213 |
| A | HIS214 |
| A | PHE215 |
| A | ILE291 |
| A | TRP394 |
| A | TRS507 |
| A | HOH711 |
| A | HOH728 |
| A | HOH819 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | THR384 |
| A | LEU385 |
| A | GLY387 |
| A | ASN395 |
| A | ILE396 |
| A | HOH607 |
| B | GOL504 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | GLN327 |
| A | HOH657 |
| A | HOH660 |
| B | HIS150 |
| B | LEU151 |
| B | HOH626 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 505 |
| Chain | Residue |
| A | ARG173 |
| A | ASN204 |
| A | ARG206 |
| A | HOH612 |
| A | HOH733 |
| A | HOH793 |
| B | HIS150 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 506 |
| Chain | Residue |
| A | LYS370 |
| A | ASP373 |
| A | HOH713 |
| A | ASP251 |
| A | VAL253 |
| A | HIS368 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue TRS A 507 |
| Chain | Residue |
| A | GLU376 |
| A | GOL502 |
| site_id | AD7 |
| Number of Residues | 20 |
| Details | binding site for Di-peptide 2RG A 501 and CYS A 354 |
| Chain | Residue |
| A | SER279 |
| A | MET280 |
| A | MET303 |
| A | THR307 |
| A | TYR308 |
| A | TYR318 |
| A | GLY332 |
| A | VAL333 |
| A | PHE334 |
| A | HIS336 |
| A | SER351 |
| A | HIS352 |
| A | GLY353 |
| A | LEU355 |
| A | ASN356 |
| A | HOH628 |
| A | HOH677 |
| A | HOH796 |
| B | PRO148 |
| B | HOH727 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 250 |
| Details | Domain: {"description":"L,D-TPase catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU01373","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01373","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23519417","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU01373","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23519417","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Site: {"description":"Binds to carbapenem drug (covalent)"} |
| Chain | Residue | Details |
