Structure of PDB 1hm8 Chain B

Receptor sequence
>1hm8B (length=458) Species: 1313 (Streptococcus pneumoniae) [Search protein sequence]
SNFAIILAAGKGTRMKSDLPKVLHKVAGISMLEHVFRSVGAIQPEKTVTV
VGHKAELVEEVLAGQTEFVTQSEQLGTGHAVMMTEPILEGLSGHTLVIAG
DTPLITGESLKNLIDFHINHKNVATILTAETDNPFGYGRIVRNDNAEVLR
IVEQKDATDFEKQIKEINTGTYVFDNERLFEALKNINTNNAQGEYYITDV
IGIFRETGEKVGAYTLKDFDESLGVNDRVALATAESVMRRRINHKHMVNG
VSFVNPEATYIDIDVEIAPEVQIEANVILKGQTKIGAETVLTNGTYVVDS
TIGAGAVITNSMIEESSVADGVTVGPYAHIRPNSSLGAQVHIGNFVEVKG
SSIGENTKAGHLTYIGNCEVGSNVNFGAGTITVNYDGKNKYKTVIGDNVF
VGSNSTIIAPVELGDNSLVGAGSTITKDVPADAIAIGRGRQINKDEYATR
LPHHPKNQ
3D structure
PDB1hm8 Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture.
ChainB
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R15
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 ACO B T383 V384 Y386 T382 V383 Y385
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003977 UDP-N-acetylglucosamine diphosphorylase activity
GO:0016740 transferase activity
GO:0016746 acyltransferase activity
GO:0016779 nucleotidyltransferase activity
GO:0019134 glucosamine-1-phosphate N-acetyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0000902 cell morphogenesis
GO:0006048 UDP-N-acetylglucosamine biosynthetic process
GO:0008360 regulation of cell shape
GO:0009058 biosynthetic process
GO:0009245 lipid A biosynthetic process
GO:0009252 peptidoglycan biosynthetic process
GO:0071555 cell wall organization
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1hm8, PDBe:1hm8, PDBj:1hm8
PDBsum1hm8
PubMed11118459
UniProtQ97R46|GLMU_STRPN Bifunctional protein GlmU (Gene Name=glmU)

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