4HCQ
Crystal structure of GLMU from mycobacterium tuberculosis in complex with glucosamine-1-phosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0000902 | biological_process | cell morphogenesis |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003977 | molecular_function | UDP-N-acetylglucosamine diphosphorylase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0009245 | biological_process | lipid A biosynthetic process |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0019134 | molecular_function | glucosamine-1-phosphate N-acetyltransferase activity |
| A | 0035635 | biological_process | entry of bacterium into host cell |
| A | 0044650 | biological_process | adhesion of symbiont to host cell |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070569 | molecular_function | uridylyltransferase activity |
| A | 0071555 | biological_process | cell wall organization |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Region: {"description":"Linker","evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"JUL-2011","submissionDatabase":"PDB data bank","title":"Structure of Mycobacterium tuberculosis GlmU in complex with Acetyl CoA.","authors":["Jagtap P.A.","Prakash B."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19237750","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23485416","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2011","submissionDatabase":"PDB data bank","title":"Structure of Mycobacterium tuberculosis GlmU in complex with Acetyl CoA.","authors":["Jagtap P.A.","Prakash B."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2012","submissionDatabase":"PDB data bank","title":"Structural snapshots of Glmu from Mycobacterium tuberculosis.","authors":["Jagtap P.A.","Verma S.K.","Prakash B."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2012","submissionDatabase":"PDB data bank","title":"Structural snapshots of Glmu from Mycobacterium tuberculosis.","authors":["Jagtap P.A.","Verma S.K.","Prakash B."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19237750","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2011","submissionDatabase":"PDB data bank","title":"Structure of Mycobacterium tuberculosis GlmU in complex with Acetyl CoA.","authors":["Jagtap P.A.","Prakash B."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19237750","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23485416","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2012","submissionDatabase":"PDB data bank","title":"Structural snapshots of Glmu from Mycobacterium tuberculosis.","authors":["Jagtap P.A.","Verma S.K.","Prakash B."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19121323","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23485416","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2011","submissionDatabase":"PDB data bank","title":"Structure of Mycobacterium tuberculosis GlmU in complex with Acetyl CoA.","authors":["Jagtap P.A.","Prakash B."]}},{"source":"PDB","id":"3SPT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HCQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23485416","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2012","submissionDatabase":"PDB data bank","title":"Structural snapshots of Glmu from Mycobacterium tuberculosis.","authors":["Jagtap P.A.","Verma S.K.","Prakash B."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2011","submissionDatabase":"PDB data bank","title":"Structure of Mycobacterium tuberculosis GlmU in complex with Acetyl CoA.","authors":["Jagtap P.A.","Prakash B."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2011","submissionDatabase":"PDB data bank","title":"Structure of Mycobacterium tuberculosis GlmU in complex with Acetyl CoA.","authors":["Jagtap P.A.","Prakash B."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)","evidences":[{"source":"PubMed","id":"20066036","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
