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2W0W

Crystal structure of Glmu from Haemophilus influenzae in complex with quinazoline inhibitor 2

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0000902biological_processcell morphogenesis
A0003824molecular_functioncatalytic activity
A0003977molecular_functionUDP-N-acetylglucosamine diphosphorylase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006048biological_processUDP-N-acetylglucosamine biosynthetic process
A0008360biological_processregulation of cell shape
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
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE LZS A 1454
ChainResidue
AALA13
AASN169
ATHR170
AGLY171
AVAL223
AGLU224
AGLY225
AGLY14
AVAL26
AGLN76
ATHR82
AALA85
ATYR103
AASP105
ATYR139

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PG4 A 1455
ChainResidue
AASN72
APHE92
AASN386
AASP388
APHE402
AALA423

Functional Information from PROSITE/UniProt
site_idPS00101
Number of Residues29
DetailsHEXAPEP_TRANSFERASES Hexapeptide-repeat containing-transferases signature. VGsdTqLvapVkVAngAtIGagTtItrdV
ChainResidueDetails
AVAL403-VAL431

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsRegion: {"description":"Linker","evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18029420","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22721802","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25262942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues11
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25262942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18029420","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25262942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18029420","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P0ACC7","evidenceCode":"ECO:0000250"},{"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
AASN386

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1lxa
ChainResidueDetails
AARG18

247536

PDB entries from 2026-01-14

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