Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3V5V

UNLIGANDED E.CLOACAE C115D MURA

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	12
Details	BINDING SITE FOR RESIDUE PEG A 501

Chain	Residue
A	ARG232
A	PRO303
A	HOH650
A	HOH654
A	ASP257
A	THR258
A	LEU259
A	ASP260
A	ALA261
A	VAL262
A	HIS299
A	PRO300

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG A 502

Chain	Residue
A	ASP260
A	ALA261

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 503

Chain	Residue
A	GLU183
A	ASN184
A	ASP211
B	LYS265
B	THR293
B	ARG295

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 505

Chain	Residue
A	VAL101
A	ALA102
A	ARG103
A	GLY149
A	ARG150

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 506

Chain	Residue
A	ASP51
A	LYS55
A	THR58

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO A 507

Chain	Residue
A	PRO27
A	PHE30
A	ALA31
A	TRP95
A	PRO99
A	VAL167
A	THR168
A	SER171

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 508

Chain	Residue
A	GLU188
A	ALA297
A	PHE302
A	PRO303
A	THR304
A	ILE327

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 509

Chain	Residue
A	PRO230
A	ASP231
A	ARG232
A	THR235
A	ALA254
A	GLN255
A	THR258

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 510

Chain	Residue
A	GLU15
A	GLU177
A	ALA408

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT A 511

Chain	Residue
A	ASN79
A	PHE80
A	SER81
A	GLN106
A	HOH703

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PGE B 501

Chain	Residue
B	ASN23
B	ALA92
B	ILE94
B	TRP95
B	VAL163
B	GLU190
B	HOH718

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO B 502

Chain	Residue
A	ASP85
B	GLU40
B	GLN42

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO B 503

Chain	Residue
B	ARG252
B	TRP279

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO B 504

Chain	Residue
B	GLU15
B	VAL16
B	THR17

site_id	BC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO B 505

Chain	Residue
A	HIS155
A	VAL157
A	GLU183
A	ARG212
B	ALA291
B	VAL292
B	THR293
B	THR320

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO B 506

Chain	Residue
B	ALA154
B	HIS155
B	THR179

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO B 507

Chain	Residue
B	GLU188
B	ARG232
B	PRO303
B	THR304
B	ASP305

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 508

Chain	Residue
B	PRO230
B	ARG232
B	THR235
B	ALA254
B	GLN255
B	THR258

site_id	CC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PEG C 501

Chain	Residue
C	HIS299
C	PRO300
C	PRO303
C	HOH661
C	ASP257
C	LEU259
C	ASP260
C	ALA261
C	VAL262

site_id	CC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 502

Chain	Residue
A	GLU139
C	GLU135
C	ILE136
C	LYS137
C	LYS144
C	SER146

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO C 503

Chain	Residue
C	ARG295
C	ALA301
C	PHE302
C	EDO504
D	ARG187

site_id	CC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 504

Chain	Residue
C	ASP260
C	ALA261
C	ALA264
C	EDO503
C	HOH690
D	ARG187

site_id	CC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO C 505

Chain	Residue
C	TRP95
C	HOH698

site_id	CC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO C 506

Chain	Residue
C	ASP49
C	THR89
C	MET90

site_id	CC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO C 507

Chain	Residue
C	LYS204
C	SER206
C	THR214
C	GLU216

site_id	CC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO C 508

Chain	Residue
A	LEU138
A	GLY141
C	GLU130
C	GLY133
C	ALA134

site_id	CC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 509

Chain	Residue
C	GLN7
C	PRO9
C	THR10
C	ASN412
C	HOH677
D	ARG252

site_id	DC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT C 510

Chain	Residue
C	ARG187
C	THR210
C	ASP211
C	HOH683
D	LYS265
D	GLU268

site_id	DC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG D 501

Chain	Residue
D	ASP260
D	ALA261
D	PRO300
D	HOH692

site_id	DC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO D 502

Chain	Residue
D	ALA21
D	LYS22
D	ASN23
D	GLU190
D	ASP231

site_id	DC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO D 503

Chain	Residue
D	LYS55

site_id	DC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO D 504

Chain	Residue
D	GLU15
D	VAL16
D	LYS405
D	ALA408

site_id	DC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO D 505

Chain	Residue
D	PRO27
D	PHE30
D	ALA31
D	TRP95
D	PRO99
D	VAL167
D	SER171

site_id	DC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO D 506

Chain	Residue
D	SER206
D	GLY207
D	ARG212
D	THR214

site_id	DC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO D 507

Chain	Residue
D	ASN43
D	ARG227
D	VAL228
D	LEU229
D	PRO230
D	ASN253

site_id	DC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO D 508

Chain	Residue
D	GLU188
D	ALA297
D	THR304
D	HOH629
D	HOH709

site_id	EC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO D 509

Chain	Residue
D	GLU15
D	ALA408

site_id	EC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO D 510

Chain	Residue
D	SER245

site_id	EC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO D 511

Chain	Residue
D	LEU229
D	PRO230
D	ASP231
D	ARG232
D	THR235
D	ALA254
D	GLN255
D	THR258

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"20392080","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22378791","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3LTH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22378791","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3SWQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00111","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20392080","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22378791","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3LTH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SWQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22378791","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3SWQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"2-(S-cysteinyl)pyruvic acid O-phosphothioketal","evidences":[{"source":"PubMed","id":"22378791","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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	ALA119	activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay
A	LEU124	electrostatic stabiliser, proton acceptor, proton donor
A	GLN309	activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ARG401	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	ALA119	activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay
B	LEU124	electrostatic stabiliser, proton acceptor, proton donor
B	GLN309	activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	ARG401	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	ALA119	activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay
C	LEU124	electrostatic stabiliser, proton acceptor, proton donor
C	GLN309	activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	ARG401	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	ALA119	activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay
D	LEU124	electrostatic stabiliser, proton acceptor, proton donor
D	GLN309	activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	ARG401	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)