Structure of PDB 1hm9 Chain B

Receptor sequence
>1hm9B (length=458) Species: 1313 (Streptococcus pneumoniae) [Search protein sequence]
SNFAIILAAGKGTRMKSDLPKVLHKVAGISMLEHVFRSVGAIQPEKTVTV
VGHKAELVEEVLAGQTEFVTQSEQLGTGHAVMMTEPILEGLSGHTLVIAG
DTPLITGESLKNLIDFHINHKNVATILTAETDNPFGYGRIVRNDNAEVLR
IVEQKDATDFEKQIKEINTGTYVFDNERLFEALKNINTNNAQGEYYITDV
IGIFRETGEKVGAYTLKDFDESLGVNDRVALATAESVMRRRINHKHMVNG
VSFVNPEATYIDIDVEIAPEVQIEANVILKGQTKIGAETVLTNGTYVVDS
TIGAGAVITNSMIEESSVADGVTVGPYAHIRPNSSLGAQVHIGNFVEVKG
SSIGENTKAGHLTYIGNCEVGSNVNFGAGTITVNYDGKNKYKTVIGDNVF
VGSNSTIIAPVELGDNSLVGAGSTITKDVPADAIAIGRGRQINKDEYATR
LPHHPKNQ
3D structure
PDB1hm9 Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture.
ChainB
Resolution1.75 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) 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 CA B D102 N227 D101 N226
BS02 CA B D398 D416 D397 D415
BS03 ACO B Y365 V384 N385 Y386 Y364 V383 N384 Y385
BS04 UD1 B L8 A10 G11 Q72 Q75 G77 T78 Y138 G139 E154 N169 T170 Y197 T199 N227 L7 A9 G10 Q71 Q74 G76 T77 Y137 G138 E153 N168 T169 Y196 T198 N226
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1hm9, PDBe:1hm9, PDBj:1hm9
PDBsum1hm9
PubMed11118459
UniProtQ97R46|GLMU_STRPN Bifunctional protein GlmU (Gene Name=glmU)

[Back to BioLiP]