Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3VCY

Structure of MurA (UDP-N-acetylglucosamine enolpyruvyl transferase), from Vibrio fischeri in complex with substrate UDP-N-acetylglucosamine and the drug fosfomycin.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005737	cellular_component	cytoplasm
A	0008360	biological_process	regulation of cell shape
A	0008760	molecular_function	UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity
A	0009252	biological_process	peptidoglycan biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
A	0019277	biological_process	UDP-N-acetylgalactosamine biosynthetic process
A	0051301	biological_process	cell division
A	0071555	biological_process	cell wall organization
B	0003824	molecular_function	catalytic activity
B	0005737	cellular_component	cytoplasm
B	0008360	biological_process	regulation of cell shape
B	0008760	molecular_function	UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity
B	0009252	biological_process	peptidoglycan biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
B	0019277	biological_process	UDP-N-acetylgalactosamine biosynthetic process
B	0051301	biological_process	cell division
B	0071555	biological_process	cell wall organization
C	0003824	molecular_function	catalytic activity
C	0005737	cellular_component	cytoplasm
C	0008360	biological_process	regulation of cell shape
C	0008760	molecular_function	UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity
C	0009252	biological_process	peptidoglycan biosynthetic process
C	0016740	molecular_function	transferase activity
C	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
C	0019277	biological_process	UDP-N-acetylgalactosamine biosynthetic process
C	0051301	biological_process	cell division
C	0071555	biological_process	cell wall organization
D	0003824	molecular_function	catalytic activity
D	0005737	cellular_component	cytoplasm
D	0008360	biological_process	regulation of cell shape
D	0008760	molecular_function	UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity
D	0009252	biological_process	peptidoglycan biosynthetic process
D	0016740	molecular_function	transferase activity
D	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
D	0019277	biological_process	UDP-N-acetylgalactosamine biosynthetic process
D	0051301	biological_process	cell division
D	0071555	biological_process	cell wall organization

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FFQ A 500

Chain	Residue
A	CYS116
A	ARG121
A	ARG398
A	PO4502
A	HOH614
A	HOH617
A	HOH876

site_id	AC2
Number of Residues	29
Details	BINDING SITE FOR RESIDUE UD1 A 501

Chain	Residue
A	ALA120
A	ARG121
A	PRO122
A	VAL123
A	ASP124
A	LEU125
A	HIS126
A	SER163
A	VAL164
A	GLY165
A	THR305
A	ASP306
A	ILE328
A	PHE329
A	ARG332
A	PO4502
A	GOL503
A	HOH603
A	HOH611
A	HOH613
A	HOH634
A	HOH648
A	HOH670
A	HOH804
A	HOH844
A	HOH868
A	HOH875
A	ASN24
A	TRP96

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 A 502

Chain	Residue
A	LYS23
A	ARG121
A	ARG398
A	FFQ500
A	UD1501
A	GOL503
A	HOH617
A	HOH618
A	HOH781

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 503

Chain	Residue
A	ARG92
A	ALA93
A	ILE95
A	HIS126
A	GLY165
A	UD1501
A	PO4502
A	HOH613

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FFQ B 500

Chain	Residue
B	ARG92
B	CYS116
B	ARG121
B	ARG398
B	HOH760
B	HOH850

site_id	AC6
Number of Residues	28
Details	BINDING SITE FOR RESIDUE UD1 B 501

Chain	Residue
B	LYS23
B	ASN24
B	TRP96
B	ALA120
B	ARG121
B	PRO122
B	VAL123
B	ASP124
B	LEU125
B	HIS126
B	SER163
B	VAL164
B	GLY165
B	THR305
B	ASP306
B	ILE328
B	PHE329
B	PO4502
B	GOL503
B	HOH611
B	HOH618
B	HOH619
B	HOH632
B	HOH685
B	HOH695
B	HOH712
B	HOH746
B	HOH786

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 B 502

Chain	Residue
B	LYS23
B	ARG121
B	UD1501
B	GOL503
B	HOH604
B	HOH727
B	HOH853

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL B 503

Chain	Residue
B	UD1501
B	PO4502
B	HOH611
B	ARG92
B	ALA93
B	ILE95
B	TRP96
B	GLY165

site_id	AC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE FFQ C 500

Chain	Residue
C	ARG92
C	GLY115
C	CYS116
C	ARG121
C	ARG398
C	PO4502
C	HOH673
C	HOH756
C	HOH859
C	HOH877
C	HOH898

site_id	BC1
Number of Residues	27
Details	BINDING SITE FOR RESIDUE UD1 C 501

Chain	Residue
C	ASN24
C	TRP96
C	ALA120
C	ARG121
C	PRO122
C	VAL123
C	ASP124
C	LEU125
C	HIS126
C	SER163
C	VAL164
C	GLY165
C	THR305
C	ASP306
C	ILE328
C	PHE329
C	PO4502
C	GOL503
C	HOH614
C	HOH625
C	HOH626
C	HOH627
C	HOH629
C	HOH630
C	HOH828
C	HOH876
C	HOH896

site_id	BC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 C 502

Chain	Residue
C	LYS23
C	ARG121
C	FFQ500
C	UD1501
C	GOL503
C	HOH736
C	HOH862
C	HOH895

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL C 503

Chain	Residue
C	ARG92
C	ALA93
C	ILE95
C	HIS126
C	GLY165
C	UD1501
C	PO4502
C	HOH629

site_id	BC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FFQ D 500

Chain	Residue
D	ARG92
D	CYS116
D	ARG121
D	ARG398
D	HOH602
D	HOH661
D	HOH920

site_id	BC5
Number of Residues	26
Details	BINDING SITE FOR RESIDUE UD1 D 501

Chain	Residue
D	ASN24
D	TRP96
D	ALA120
D	ARG121
D	PRO122
D	VAL123
D	ASP124
D	LEU125
D	HIS126
D	SER163
D	VAL164
D	GLY165
D	THR305
D	ASP306
D	ILE328
D	PHE329
D	PO4502
D	GOL503
D	HOH616
D	HOH617
D	HOH621
D	HOH622
D	HOH629
D	HOH818
D	HOH849
D	HOH922

site_id	BC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 D 502

Chain	Residue
D	LYS23
D	ARG121
D	ARG398
D	UD1501
D	GOL503
D	HOH601
D	HOH603
D	HOH716
D	HOH918

site_id	BC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL D 503

Chain	Residue
D	ARG92
D	ALA93
D	ILE95
D	ARG121
D	GLY165
D	UD1501
D	PO4502
D	HOH622

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000255\|HAMAP-Rule:MF_00111

Chain	Residue	Details
A	CYS116
B	CYS116
C	CYS116
D	CYS116

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000305\|PubMed:22505403, ECO:0007744\|PDB:3VCY

Chain	Residue	Details
A	LYS23
A	LYS161
B	LYS23
B	LYS161
C	LYS23
C	LYS161
D	LYS23
D	LYS161

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00111

Chain	Residue	Details
A	ARG92
B	ARG92
C	ARG92
D	ARG92

site_id	SWS_FT_FI4
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:22505403, ECO:0007744\|PDB:3VCY

Chain	Residue	Details
A	ARG121
D	ARG121
D	ASP306
D	ILE328
A	ASP306
A	ILE328
B	ARG121
B	ASP306
B	ILE328
C	ARG121
C	ASP306
C	ILE328

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000255\|HAMAP-Rule:MF_00111

Chain	Residue	Details
A	CYS116
B	CYS116
C	CYS116
D	CYS116

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)