Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4E7B

E. cloacae MurA in complex with UDP-glucose

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 EDO A 501

Chain	Residue
A	ARG187
A	THR210
A	ASP211
A	HOH719
A	HOH814
B	LYS265
B	GLU268

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 502

Chain	Residue
A	GLY107
A	GLN108
A	HOH741
A	PHE80
A	GLN106

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO A 503

Chain	Residue
A	ARG187
A	ASP211
A	PRO298
A	HIS299
A	PRO300
A	HOH745
B	EDO504
B	HOH723
B	HOH853

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 504

Chain	Residue
A	ILE339
A	ALA345
A	GLU346
A	ILE347
A	HOH831

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 505

Chain	Residue
A	HIS344
A	VAL357
A	GLU358
A	HOH789

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 506

Chain	Residue
A	ALA92
A	TRP95
A	HIS125
A	GLY164
A	HOH728
A	HOH857

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 507

Chain	Residue
A	GLY153
A	GLY178
A	THR179
C	LYS55

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 508

Chain	Residue
A	LYS46
A	LEU47
A	LYS48
A	ASP51
A	HOH827

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 509

Chain	Residue
A	VAL161
A	ALA186
A	GLU188
A	PRO298
A	UPG513
A	HOH707
A	HOH752

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 510

Chain	Residue
A	ARG295
A	ALA297
A	ALA301
A	PHE302
B	EDO501
B	EDO514
B	HOH692

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 511

Chain	Residue
A	GLN59
A	ASN78
A	ASN79

site_id	BC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE UPG A 513

Chain	Residue
A	PRO121
A	VAL122
A	ASP123
A	LEU124
A	HIS125
A	VAL161
A	SER162
A	VAL163
A	GLY164
A	ASP305
A	EDO509
A	HOH728
A	HOH793
A	HOH857
A	HOH908
A	HOH913

site_id	BC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO B 501

Chain	Residue
A	LYS265
A	GLU268
A	EDO510
A	HOH712
B	ARG187
B	THR210
B	ASP211
B	EDO514

site_id	BC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO B 502

Chain	Residue
B	GLU65

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO B 503

Chain	Residue
B	GLN42
B	ARG227
B	HOH716

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 504

Chain	Residue
A	PRO298
A	EDO503
A	HOH707
B	ARG295
B	HOH714
B	HOH853

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 505

Chain	Residue
B	VAL122
B	EDO506
B	UPG516
B	ARG91
B	ARG120
B	PRO121

site_id	BC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO B 506

Chain	Residue
B	ALA92
B	TRP95
B	GLY164
B	EDO505
B	UPG516
B	HOH673
B	HOH735

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO B 507

Chain	Residue
B	ILE339
B	ALA343
B	HIS344
B	ALA345
B	GLU346

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO B 508

Chain	Residue
A	HOH645
A	HOH774
B	LYS290
B	HOH729

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 509

Chain	Residue
B	VAL161
B	ALA186
B	ARG187
B	GLU188
B	HOH767
B	HOH787

site_id	CC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO B 510

Chain	Residue
B	VAL199
B	ALA203
B	HOH705
B	HOH777
B	HOH891

site_id	CC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO B 511

Chain	Residue
B	LYS63
B	VAL64
B	GLU65
B	TRP71
B	ASP73
B	HOH715
B	HOH842

site_id	CC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO B 512

Chain	Residue
B	GLN7
B	TYR84
B	ASP85
B	LYS88
B	THR386

site_id	CC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO B 513

Chain	Residue
B	PRO300
B	EDO514
B	HOH849

site_id	CC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO B 514

Chain	Residue
A	EDO510
B	ARG187
B	PRO300
B	EDO501
B	EDO513

site_id	CC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 515

Chain	Residue
B	HIS344
B	HIS355
B	HOH725
C	THR58
C	GLN59
C	HOH635

site_id	DC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE UPG B 516

Chain	Residue
B	ARG91
B	ARG120
B	PRO121
B	VAL122
B	ASP123
B	LEU124
B	HIS125
B	VAL161
B	SER162
B	VAL163
B	GLY164
B	EDO505
B	EDO506
B	HOH673
B	HOH735
B	HOH895
B	HOH896

site_id	DC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO C 501

Chain	Residue
A	GLY149
A	ARG150
A	HOH907
C	MET1
C	ASP2
C	TYR393
C	ARG415
C	HOH641
C	HOH873

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

Chain	Residue
C	ALA21
C	LYS22
C	ASN23
C	GLU190
C	ASP231

site_id	DC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE EDO C 503

Chain	Residue
C	VAL87
C	ARG91
C	SER93
C	ILE94
C	VAL109
C	SER110
C	LEU111
C	PRO112
C	VAL122
C	HOH766

site_id	DC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO C 504

Chain	Residue
A	PHE104
A	GLY105
A	VAL147
C	HOH657
C	HOH800

site_id	DC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO C 505

Chain	Residue
C	HIS394
C	ARG397
C	ACT513
C	HOH697

site_id	DC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 506

Chain	Residue
A	ASN330
C	PHE328
C	GLU329
C	ASN330
C	ARG331
C	PHE332

site_id	DC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO C 507

Chain	Residue
C	ARG252
C	TRP279

site_id	DC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 508

Chain	Residue
C	ALA92
C	TRP95
C	HIS125
C	GLY164
C	UPG514
C	HOH826

site_id	EC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO C 509

Chain	Residue
C	PRO38
C	GLY224
C	HOH844
C	HOH874
C	HOH881

site_id	EC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO C 510

Chain	Residue
C	MET341
C	GLY342
C	LYS359
C	LEU360
C	SER361
D	VAL64
D	GLU65
D	EDO503

site_id	EC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO C 511

Chain	Residue
C	PHE104
C	GLY105
C	VAL147
C	GLY149

site_id	EC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO C 512

Chain	Residue
C	GLU15
C	VAL16
C	THR17
C	HOH700
C	HOH736
C	HOH817
D	TYR84
D	ASP85

site_id	EC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT C 513

Chain	Residue
C	TYR393
C	HIS394
C	ARG397
C	EDO505

site_id	EC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE UPG C 514

Chain	Residue
C	ARG91
C	PRO121
C	VAL122
C	ASP123
C	LEU124
C	HIS125
C	VAL161
C	SER162
C	VAL163
C	GLY164
C	EDO508
C	HOH826

site_id	EC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO D 501

Chain	Residue
C	ASP211
D	LYS265
D	ARG295
D	ALA301
D	PHE302
D	HOH803

site_id	EC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO D 502

Chain	Residue
A	PHE127
A	GLU130
A	LYS131
D	GLU140
D	HOH772

site_id	EC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO D 503

Chain	Residue
C	EDO510
D	THR58
D	THR62
D	LYS63
D	VAL64

site_id	FC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO D 504

Chain	Residue
D	ARG295
D	ALA297
D	ALA301
D	HOH779

site_id	FC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE UPG D 505

Chain	Residue
D	ASN23
D	ARG120
D	PRO121
D	VAL122
D	ASP123
D	LEU124
D	HIS125
D	LYS160
D	VAL161
D	SER162
D	VAL163
D	GLY164
D	ASP305
D	PHE328
D	HOH632
D	HOH692
D	HOH726
D	HOH792
D	HOH794

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	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)