1G95

CRYSTAL STRUCTURE OF S.PNEUMONIAE GLMU, APO FORM

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0000902	biological_process	cell morphogenesis
A	0003977	molecular_function	UDP-N-acetylglucosamine diphosphorylase activity
A	0005737	cellular_component	cytoplasm
A	0006048	biological_process	UDP-N-acetylglucosamine biosynthetic process
A	0008360	biological_process	regulation of cell shape
A	0009058	biological_process	biosynthetic process
A	0009245	biological_process	lipid A biosynthetic process
A	0009252	biological_process	peptidoglycan biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016746	molecular_function	acyltransferase activity
A	0016779	molecular_function	nucleotidyltransferase activity
A	0019134	molecular_function	glucosamine-1-phosphate N-acetyltransferase activity
A	0046872	molecular_function	metal ion binding
A	0071555	biological_process	cell wall organization

Functional Information from PROSITE/UniProt

site_id	PS00101
Number of Residues	29
Details	HEXAPEP_TRANSFERASES Hexapeptide-repeat containing-transferases signature. VGsnStIiapVeLGdnSlVGagStItkdV

Chain	Residue	Details
A	VAL402-VAL430

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01631

Chain	Residue	Details
A	HIS362

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:11118459, ECO:0000269|PubMed:11124906

Chain	Residue	Details
A	LEU8
A	GLN72
A	GLY77
A	GLY139
A	GLU154
A	ASN169

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site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:11118459

Chain	Residue	Details
A	LYS22
A	ASN227
A	ASN385

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site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:11118459, ECO:0000269|PubMed:11124906

Chain	Residue	Details
A	GLY101

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site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:11124906, ECO:0007744|PDB:1G97

Chain	Residue	Details
A	ASP102

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site_id	SWS_FT_FI6
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631

Chain	Residue	Details
A	ARG332
A	LYS350
A	TYR365
A	ASN376
A	ALA379
A	SER404
A	ALA422
A	ARG439

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1lxa

Chain	Residue	Details
A	SER373

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site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1lxa

Chain	Residue	Details
A	ARG15

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