Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1HM0

CRYSTAL STRUCTURE OF S.PNEUMONIAE N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE, GLMU

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0000902biological_processcell morphogenesis
A0003824molecular_functioncatalytic activity
A0003977molecular_functionUDP-N-acetylglucosamine diphosphorylase activity
A0005737cellular_componentcytoplasm
A0006048biological_processUDP-N-acetylglucosamine biosynthetic process
A0008360biological_processregulation of cell shape
A0009058biological_processbiosynthetic process
A0009245biological_processlipid A biosynthetic process
A0009252biological_processpeptidoglycan biosynthetic process
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0019134molecular_functionglucosamine-1-phosphate N-acetyltransferase activity
A0046872molecular_functionmetal ion binding
A0071555biological_processcell wall organization
B0000287molecular_functionmagnesium ion binding
B0000902biological_processcell morphogenesis
B0003824molecular_functioncatalytic activity
B0003977molecular_functionUDP-N-acetylglucosamine diphosphorylase activity
B0005737cellular_componentcytoplasm
B0006048biological_processUDP-N-acetylglucosamine biosynthetic process
B0008360biological_processregulation of cell shape
B0009058biological_processbiosynthetic process
B0009245biological_processlipid A biosynthetic process
B0009252biological_processpeptidoglycan biosynthetic process
B0016020cellular_componentmembrane
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0016779molecular_functionnucleotidyltransferase activity
B0019134molecular_functionglucosamine-1-phosphate N-acetyltransferase activity
B0046872molecular_functionmetal ion binding
B0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 901
ChainResidue
AASN405
AASN405
AASN405

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA A 902
ChainResidue
AASP398
AHOH952

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA B 901
ChainResidue
BASN405
BASN405
BASN405

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CA B 902
ChainResidue
BASP398

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA B 903
ChainResidue
BHOH1048
BHOH1048
BHOH1048

Functional Information from PROSITE/UniProt
site_idPS00101
Number of Residues29
DetailsHEXAPEP_TRANSFERASES Hexapeptide-repeat containing-transferases signature. VGsnStIiapVeLGdnSlVGagStItkdV
ChainResidueDetails
AVAL402-VAL430

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsRegion: {"description":"Linker","evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11118459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11124906","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11118459","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11118459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11124906","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11124906","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1G97","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1lxa
ChainResidueDetails
ASER373

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1lxa
ChainResidueDetails
BSER373

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1lxa
ChainResidueDetails
AARG15

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1lxa
ChainResidueDetails
BARG15

239149

PDB entries from 2025-07-23

PDB statisticsPDBj update infoContact PDBjnumon