Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1HV9

STRUCTURE OF E. COLI GLMU: ANALYSIS OF PYROPHOSPHORYLASE AND ACETYLTRANSFERASE ACTIVE SITES

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0000902	biological_process	cell morphogenesis
A	0003824	molecular_function	catalytic activity
A	0003977	molecular_function	UDP-N-acetylglucosamine diphosphorylase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006048	biological_process	UDP-N-acetylglucosamine biosynthetic process
A	0008360	biological_process	regulation of cell shape
A	0009245	biological_process	lipid A biosynthetic process
A	0009252	biological_process	peptidoglycan biosynthetic process
A	0016020	cellular_component	membrane
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	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0071555	biological_process	cell wall organization
B	0000287	molecular_function	magnesium ion binding
B	0000902	biological_process	cell morphogenesis
B	0003824	molecular_function	catalytic activity
B	0003977	molecular_function	UDP-N-acetylglucosamine diphosphorylase activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006048	biological_process	UDP-N-acetylglucosamine biosynthetic process
B	0008360	biological_process	regulation of cell shape
B	0009245	biological_process	lipid A biosynthetic process
B	0009252	biological_process	peptidoglycan biosynthetic process
B	0016020	cellular_component	membrane
B	0016740	molecular_function	transferase activity
B	0016746	molecular_function	acyltransferase activity
B	0016779	molecular_function	nucleotidyltransferase activity
B	0019134	molecular_function	glucosamine-1-phosphate N-acetyltransferase activity
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0071555	biological_process	cell wall organization

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CO B 9027

Chain	Residue
B	LYS25
B	ASP105
B	ASN227
B	UD13002
B	HOH5026
B	HOH5027

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CO B 9028

Chain	Residue
B	HOH5045
B	HOH5045
B	HOH5045
B	CO9029
B	CO9029
B	CO9029
B	ASP406
B	ASP406
B	ASP406

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CO B 9029

Chain	Residue
B	ASP406
B	ASP406
B	ASP406
B	HOH6868
B	HOH6868
B	HOH6868
B	CO9028
B	CO9028
B	CO9028

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CO A 9030

Chain	Residue
A	ASP406
A	ASP406
A	ASP406
A	HOH6867
A	HOH6867
A	HOH6867
A	CO9031
A	CO9031
A	CO9031

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CO A 9031

Chain	Residue
A	ASP406
A	ASP406
A	ASP406
A	HOH6036
A	HOH6036
A	HOH6036
A	CO9030
A	CO9030
A	CO9030

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE COA A 2001

Chain	Residue
A	CYS385
A	TYR387
A	SER405
A	ALA422
A	ALA423
A	ARG440
A	LYS446
A	HOH4037
A	HOH5142
A	HOH5458
B	ARG429

site_id	AC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE COA B 2002

Chain	Residue
A	ARG429
B	CYS385
B	TYR387
B	GLY404
B	SER405
B	ALA422
B	ALA423
B	ARG440
B	LYS446
B	TRP449
B	HOH4051
B	HOH5166

site_id	AC8
Number of Residues	19
Details	BINDING SITE FOR RESIDUE UD1 A 3001

Chain	Residue
A	LEU11
A	ALA13
A	GLY14
A	GLN76
A	GLN79
A	LEU80
A	GLY81
A	THR82
A	TYR103
A	ASP105
A	GLY140
A	GLU154
A	ASN169
A	THR170
A	TYR197
A	ILE198
A	THR199
A	HOH5272
A	HOH5373

site_id	AC9
Number of Residues	24
Details	BINDING SITE FOR RESIDUE UD1 B 3002

Chain	Residue
B	ASN169
B	THR199
B	ASN227
B	HOH5006
B	HOH5026
B	HOH5027
B	HOH5120
B	HOH5264
B	CO9027
B	LEU11
B	ALA12
B	ALA13
B	GLY14
B	LYS25
B	GLN76
B	GLN79
B	GLY81
B	THR82
B	TYR103
B	GLY104
B	ASP105
B	TYR139
B	GLY140
B	GLU154

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL403-VAL431

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	40
Details	Region: {"description":"Linker","evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10428949","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8555230","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10428949","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11329257","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17473010","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17473010","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2OI5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11329257","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17473010","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11329257","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17473010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21984832","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17473010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21984832","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 10428949

Chain	Residue	Details
A	ARG18

site_id	CSA2
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 10428949

Chain	Residue	Details
B	ARG18

site_id	MCSA1
Number of Residues	1
Details	M-CSA 811

Chain	Residue	Details
A	ARG18	electrostatic stabiliser

site_id	MCSA2
Number of Residues	1
Details	M-CSA 811

Chain	Residue	Details
B	ARG18	electrostatic stabiliser

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)