Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3SWQ

E. Cloacae MurA in complex with Enolpyruvyl-UNAG

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PGE A 420

Chain	Residue
A	GLN108
A	GLU140
A	TYR142
A	LYS144

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PEG A 421

Chain	Residue
A	ARG220
A	EDO433
A	HOH492
A	HOH610
A	HOH672
A	GLU36
A	ALA102
A	ARG103
A	ARG150
A	GLU219

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 422

Chain	Residue
A	ARG120
A	HIS125
A	GLY164
A	EPU440
A	HOH458
A	HOH491
A	HOH581

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 423

Chain	Residue
A	ASN79
A	SER81
A	PRO83
A	HIS285
A	GLY286
A	HOH501

site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO A 424

Chain	Residue
A	ARG252

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 425

Chain	Residue
A	ILE205
A	SER206
A	GLN208
A	HOH655
A	HOH724

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 426

Chain	Residue
A	LYS160
A	VAL161
A	ARG295
A	ALA297
A	HOH473
A	HOH737
A	HOH812

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 427

Chain	Residue
A	ALA116
A	MET333
A	HOH609
A	HOH815
A	HOH826

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 428

Chain	Residue
A	VAL192
A	ASN196
A	GLN208
A	HOH849

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 429

Chain	Residue
A	ILE126
A	ILE339
A	HIS344
A	EDO434
A	HOH460

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 430

Chain	Residue
A	GLU37
A	ALA200
A	LEU201
A	GLY202
A	GLY222
A	GLY223
A	HOH813

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 431

Chain	Residue
A	ALA154
A	HIS155
A	THR179

site_id	BC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO A 432

Chain	Residue
A	GLY118
A	ALA119
A	ILE327
A	PHE328
A	GLU329
A	ASN330
A	HOH626
A	HOH838
A	HOH850

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 433

Chain	Residue
A	GLU36
A	ARG103
A	PEG421

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 434

Chain	Residue
A	PRO121
A	VAL122
A	EDO429
A	HOH484

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 435

Chain	Residue
A	GLN7
A	GLY8
A	PRO9
A	THR10
A	LYS63
A	VAL64
A	ASN412

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 436

Chain	Residue
A	VAL199
A	GLY202
A	ALA203
A	HOH648
A	HOH795

site_id	BC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 437

Chain	Residue
A	GLY133
A	HOH470
A	HOH811

site_id	CC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 438

Chain	Residue
A	GLU65
A	TRP71
A	HOH624

site_id	CC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT A 439

Chain	Residue
A	GLU329
A	ILE347
A	GLU348
A	SER349
A	HOH756
A	LYS160

site_id	CC3
Number of Residues	31
Details	BINDING SITE FOR RESIDUE EPU A 440

Chain	Residue
A	LYS22
A	ASN23
A	TRP95
A	ALA119
A	ARG120
A	PRO121
A	VAL122
A	ASP123
A	LEU124
A	HIS125
A	LYS160
A	SER162
A	VAL163
A	GLY164
A	THR304
A	ASP305
A	ILE327
A	PHE328
A	LEU370
A	EDO422
A	HOH452
A	HOH458
A	HOH471
A	HOH477
A	HOH497
A	HOH520
A	HOH551
A	HOH628
A	HOH638
A	HOH661
A	HOH704

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000269\|PubMed:20392080, ECO:0000269\|PubMed:22378791, ECO:0007744\|PDB:3LTH

Chain	Residue	Details
A	CYS115

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000305\|PubMed:22378791, ECO:0007744\|PDB:3SWQ

Chain	Residue	Details
A	LYS22

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00111

Chain	Residue	Details
A	ARG91

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

Chain	Residue	Details
A	ARG120
A	ASP305
A	ILE327

site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:22378791, ECO:0007744\|PDB:3SWQ

Chain	Residue	Details
A	LYS160

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000269\|PubMed:22378791

Chain	Residue	Details
A	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

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