Structure of PDB 4hcq Chain A

Receptor sequence
>4hcqA (length=452) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence]
DTAVLVLAAGPGTRMRSDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVV
LGHDHQRIAPLVGELADTLGRTIDVALQDRPLGTGHAVLCGLSALPDDYA
GNVVVTSGDTPLLDADTLADLIATHRAVSAAVTVLTTTLDDPFGYGRILR
TQDHEVMAIVEQTDATPSQREIREVNAGVYAFDIAALRSALSRLSSNNAQ
QELYLTDVIAILRSDGQTVHASHVDDSALVAGVNNRVQLAELASELNRRV
VAAHQLAGVTVVDPATTWIDVDVTIGRDTVIHPGTQLLGRTQIGGRCVVG
PDTTLTDVAVGDGASVVRTHGSSSSIGDGAAVGPFTYLRPGTALGADGKL
GAFVEVKNSTIGTGTKVPHLTYVGDADIGEYSNIGASSVFVNRTTVGSHV
RTGSDTMFVAPVTIGDGAYTGAGTVVREDVPPGALAVSAGPQRNIENWVQ
RK
3D structure
PDB4hcq Crystal structures identify an atypical two-metal-ion mechanism for uridyltransfer in GlmU: its significance to sugar nucleotidyl transferases
ChainA
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) R19
Catalytic site (residue number reindexed from 1) R14
Enzyme Commision number 2.3.1.157: glucosamine-1-phosphate N-acetyltransferase.
2.7.7.23: UDP-N-acetylglucosamine diphosphorylase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 GN1 A R344 K362 Y377 N397 R339 K357 Y372 N392
BS02 GN1 A T89 Y150 G151 E166 N181 A182 T211 T84 Y145 G146 E161 N176 A177 T206
BS03 MG A D114 N239 D109 N234
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003977 UDP-N-acetylglucosamine diphosphorylase activity
GO:0005515 protein binding
GO:0016746 acyltransferase activity
GO:0016779 nucleotidyltransferase activity
GO:0019134 glucosamine-1-phosphate N-acetyltransferase activity
GO:0046872 metal ion binding
GO:0070569 uridylyltransferase activity
Biological Process
GO:0000902 cell morphogenesis
GO:0006048 UDP-N-acetylglucosamine biosynthetic process
GO:0008360 regulation of cell shape
GO:0009245 lipid A biosynthetic process
GO:0009252 peptidoglycan biosynthetic process
GO:0035635 entry of bacterium into host cell
GO:0044650 adhesion of symbiont to host cell
GO:0071555 cell wall organization
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4hcq, PDBe:4hcq, PDBj:4hcq
PDBsum4hcq
PubMed23485416
UniProtP9WMN3|GLMU_MYCTU Bifunctional protein GlmU (Gene Name=glmU)

[Back to BioLiP]