5D7H
X-RAY CRYSTAL STRUCTURE OF L,D TRANSPEPTIDASE 2 FROM MYCOBACTERIUM TUBERCULOSIS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0018104 | biological_process | peptidoglycan-protein cross-linking |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071555 | biological_process | cell wall organization |
| A | 0071972 | molecular_function | peptidoglycan L,D-transpeptidase activity |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0018104 | biological_process | peptidoglycan-protein cross-linking |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071555 | biological_process | cell wall organization |
| B | 0071972 | molecular_function | peptidoglycan L,D-transpeptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 501 |
| Chain | Residue |
| A | ARG104 |
| A | PRO107 |
| A | SO4505 |
| A | HOH619 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 502 |
| Chain | Residue |
| A | GLY234 |
| A | GLU235 |
| A | HOH610 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 503 |
| Chain | Residue |
| A | ARG122 |
| B | PRO311 |
| B | VAL312 |
| B | ASN313 |
| A | ARG99 |
| A | GLU116 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 504 |
| Chain | Residue |
| A | ARG297 |
| A | ARG371 |
| A | HOH604 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 505 |
| Chain | Residue |
| A | SER106 |
| A | ARG111 |
| A | SO4501 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 506 |
| Chain | Residue |
| A | HIS336 |
| A | TRP340 |
| A | SER351 |
| A | HIS352 |
| A | CYS354 |
| A | ASN356 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 507 |
| Chain | Residue |
| A | ASN177 |
| A | ASN204 |
| A | ASN205 |
| A | HOH605 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue GOL A 508 |
| Chain | Residue |
| A | GLU176 |
| A | ARG206 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 509 |
| Chain | Residue |
| A | HIS300 |
| B | HIS150 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 501 |
| Chain | Residue |
| B | ARG297 |
| B | ARG371 |
| B | HOH604 |
| B | HOH628 |
| B | HOH690 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 502 |
| Chain | Residue |
| B | ASN177 |
| B | ASN205 |
| B | ARG206 |
| B | HOH613 |
| B | HOH681 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 503 |
| Chain | Residue |
| B | HIS336 |
| B | TRP340 |
| B | SER351 |
| B | HIS352 |
| B | CYS354 |
| B | ASN356 |
| B | HOH608 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 504 |
| Chain | Residue |
| B | ARG104 |
| B | SER106 |
| B | ARG111 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 505 |
| Chain | Residue |
| B | ARG123 |
| B | THR142 |
| B | SER358 |
| B | PRO359 |
| B | SER360 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 506 |
| Chain | Residue |
| B | ASN205 |
| B | HOH611 |
| B | HOH681 |
| site_id | AD7 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 B 507 |
| Chain | Residue |
| B | LYS189 |
| site_id | AD8 |
| Number of Residues | 2 |
| Details | binding site for residue GOL B 508 |
| Chain | Residue |
| B | GLU176 |
| B | ARG206 |
| site_id | AD9 |
| Number of Residues | 2 |
| Details | binding site for residue GOL B 509 |
| Chain | Residue |
| B | GLU271 |
| B | VAL272 |
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":"23103390","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":"23103390","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Site: {"description":"Binds to carbapenem drug (covalent)","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
