4J72
Crystal Structure of polyprenyl-phosphate N-acetyl hexosamine 1-phosphate transferase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0008963 | molecular_function | phospho-N-acetylmuramoyl-pentapeptide-transferase activity |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016780 | molecular_function | phosphotransferase activity, for other substituted phosphate groups |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0044038 | biological_process | cell wall macromolecule biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051301 | biological_process | cell division |
| A | 0051992 | molecular_function | UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity |
| A | 0071555 | biological_process | cell wall organization |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0008963 | molecular_function | phospho-N-acetylmuramoyl-pentapeptide-transferase activity |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016780 | molecular_function | phosphotransferase activity, for other substituted phosphate groups |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0044038 | biological_process | cell wall macromolecule biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051301 | biological_process | cell division |
| B | 0051992 | molecular_function | UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity |
| B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NI A 401 |
| Chain | Residue |
| A | HIS324 |
| A | HIS325 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NI A 402 |
| Chain | Residue |
| A | HIS326 |
| A | GLU328 |
| A | GLU334 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG A 403 |
| Chain | Residue |
| A | ASP265 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG B 401 |
| Chain | Residue |
| B | ASP265 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=Helix 1","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 34 |
| Details | Transmembrane: {"description":"Helical; Name=Helix 2","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 82 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 42 |
| Details | Transmembrane: {"description":"Helical; Name=Helix 3","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 50 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 42 |
| Details | Transmembrane: {"description":"Helical; Name=Helix 4","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 42 |
| Details | Transmembrane: {"description":"Helical; Name=Helix 5","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=Helix 6","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 42 |
| Details | Transmembrane: {"description":"Helical; Name=Helix 7","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 30 |
| Details | Transmembrane: {"description":"Helical; Name=Helix 8","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 50 |
| Details | Transmembrane: {"description":"Helical; Name=Helix 9","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=Helix 10","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 17 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27088606","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5CKR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
