Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4E7C

E. cloacae MurA in complex with UTP

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	3
Details	BINDING SITE FOR RESIDUE EDO A 501

Chain	Residue
A	PRO298
A	HIS299
B	ALA297

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 502

Chain	Residue
A	TYR226
A	ARG227
A	EDO503
A	HOH712
A	HOH767
A	HOH789

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 503

Chain	Residue
A	ASN43
A	ARG227
A	VAL228
A	PRO230
A	ASN253
A	EDO502
A	HOH789

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT A 504

Chain	Residue
A	ARG91
A	TRP95
A	GLY164
A	UTP506

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT A 505

Chain	Residue
A	ASP404
A	LYS405
A	HOH845

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE UTP A 506

Chain	Residue
A	ARG91
A	PRO121
A	VAL122
A	ASP123
A	LEU124
A	HIS125
A	LYS160
A	SER162
A	VAL163
A	GLY164
A	ACT504
A	HOH640
A	HOH760

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO B 501

Chain	Residue
B	ALA21
B	LYS22
B	ASN23
B	ASP231
B	ILE233
B	ARG371
B	HOH734

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT B 502

Chain	Residue
A	LYS265
A	GLU268
B	ARG187
B	THR210
B	ASP211

site_id	AC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE UTP B 503

Chain	Residue
B	ARG91
B	PRO121
B	VAL122
B	ASP123
B	LEU124
B	HIS125
B	LYS160
B	SER162
B	VAL163
B	GLY164
B	HOH723
B	HOH790

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO C 501

Chain	Residue
B	GLU177
C	ARG397

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO C 502

Chain	Residue
C	PRO9
C	THR10
C	ARG11
C	SER245
C	ILE382

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO C 503

Chain	Residue
B	ILE117
C	ALA291
C	VAL292
C	THR293
C	THR320
C	HOH638
D	HIS155
D	VAL157
D	GLU183

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO C 504

Chain	Residue
C	GLY224
C	VAL225

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO C 505

Chain	Residue
C	GLU177
C	GLY178
C	GLY217

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT C 506

Chain	Residue
C	ALA92
C	ILE94
C	TRP95
C	GLY164

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO D 501

Chain	Residue
D	ASN43
D	VAL44
D	LYS46
D	GLY68
D	GLU400

site_id	BC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO D 502

Chain	Residue
A	GLU329
A	ASN330
D	GLU325
D	PHE328
D	GLU329
D	ASN330
D	ARG331
D	PHE332

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO D 503

Chain	Residue
D	VAL163
D	GLY164
D	HOH723
D	SER162

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT D 504

Chain	Residue
C	HOH671
D	IAS67
D	GLY68
D	SER69

site_id	CC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACT D 505

Chain	Residue
B	GLU130
D	LEU138
D	GLU139
D	GLU140
D	GLY141
D	TYR142
D	HOH694

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000269\|PubMed:20392080, ECO:0000269\|PubMed:22378791, ECO:0007744\|PDB:3LTH

Chain	Residue	Details
A	CYS115
B	CYS115
C	CYS115
D	CYS115

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305\|PubMed:22378791, ECO:0007744\|PDB:3SWQ

Chain	Residue	Details
A	LYS22
B	LYS22
C	LYS22
D	LYS22

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

Chain	Residue	Details
A	ARG91
B	ARG91
C	ARG91
D	ARG91

site_id	SWS_FT_FI4
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:20392080, ECO:0000269\|PubMed:22378791, ECO:0007744\|PDB:3LTH, ECO:0007744\|PDB:3SWQ

Chain	Residue	Details
A	ARG120
D	ARG120
D	ASP305
D	ILE327
A	ASP305
A	ILE327
B	ARG120
B	ASP305
B	ILE327
C	ARG120
C	ASP305
C	ILE327

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:22378791, ECO:0007744\|PDB:3SWQ

Chain	Residue	Details
A	LYS160
B	LYS160
C	LYS160
D	LYS160

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000269\|PubMed:22378791

Chain	Residue	Details
A	CYS115
B	CYS115
C	CYS115
D	CYS115

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 369

Chain	Residue	Details
A	LYS22	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor
A	ASN23	electrostatic stabiliser, hydrogen bond donor
A	CYS115	activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay
A	ARG120	electrostatic stabiliser, proton acceptor, proton donor
A	ASP305	activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ARG397	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA2
Number of Residues	6
Details	M-CSA 369

Chain	Residue	Details
B	LYS22	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor
B	ASN23	electrostatic stabiliser, hydrogen bond donor
B	CYS115	activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay
B	ARG120	electrostatic stabiliser, proton acceptor, proton donor
B	ASP305	activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	ARG397	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA3
Number of Residues	6
Details	M-CSA 369

Chain	Residue	Details
C	LYS22	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor
C	ASN23	electrostatic stabiliser, hydrogen bond donor
C	CYS115	activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay
C	ARG120	electrostatic stabiliser, proton acceptor, proton donor
C	ASP305	activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	ARG397	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA4
Number of Residues	6
Details	M-CSA 369

Chain	Residue	Details
D	LYS22	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor
D	ASN23	electrostatic stabiliser, hydrogen bond donor
D	CYS115	activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay
D	ARG120	electrostatic stabiliser, proton acceptor, proton donor
D	ASP305	activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	ARG397	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor

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