Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7KR9

Bifunctional enzyme GlmU bound to Zn(II)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0000902biological_processcell morphogenesis
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
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 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 Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01631
ChainResidueDetails
AHIS362

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631
ChainResidueDetails
ALEU8
AARG332
ALYS350
ATYR365
AASN376
AALA379
AASN385
ASER404
AALA422
AARG439
ALYS22
AGLN72
AGLY77
AASP102
AGLY139
AGLU154
AASN169
AASN227

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon