Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1RYW

C115S MurA liganded with reaction products

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
E	0003824	molecular_function	catalytic activity
E	0005737	cellular_component	cytoplasm
E	0008360	biological_process	regulation of cell shape
E	0008760	molecular_function	UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity
E	0009252	biological_process	peptidoglycan biosynthetic process
E	0016740	molecular_function	transferase activity
E	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
E	0019277	biological_process	UDP-N-acetylgalactosamine biosynthetic process
E	0051301	biological_process	cell division
E	0071555	biological_process	cell wall organization
F	0003824	molecular_function	catalytic activity
F	0005737	cellular_component	cytoplasm
F	0008360	biological_process	regulation of cell shape
F	0008760	molecular_function	UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity
F	0009252	biological_process	peptidoglycan biosynthetic process
F	0016740	molecular_function	transferase activity
F	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
F	0019277	biological_process	UDP-N-acetylgalactosamine biosynthetic process
F	0051301	biological_process	cell division
F	0071555	biological_process	cell wall organization
G	0003824	molecular_function	catalytic activity
G	0005737	cellular_component	cytoplasm
G	0008360	biological_process	regulation of cell shape
G	0008760	molecular_function	UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity
G	0009252	biological_process	peptidoglycan biosynthetic process
G	0016740	molecular_function	transferase activity
G	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
G	0019277	biological_process	UDP-N-acetylgalactosamine biosynthetic process
G	0051301	biological_process	cell division
G	0071555	biological_process	cell wall organization
H	0003824	molecular_function	catalytic activity
H	0005737	cellular_component	cytoplasm
H	0008360	biological_process	regulation of cell shape
H	0008760	molecular_function	UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity
H	0009252	biological_process	peptidoglycan biosynthetic process
H	0016740	molecular_function	transferase activity
H	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
H	0019277	biological_process	UDP-N-acetylgalactosamine biosynthetic process
H	0051301	biological_process	cell division
H	0071555	biological_process	cell wall organization

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 A 2461

Chain	Residue
A	LYS22
A	ARG120
A	ARG397
A	HOH682
A	HOH761
A	HOH810
A	EPU2450
A	GOL2471

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 B 3461

Chain	Residue
B	ARG120
B	ARG397
B	HOH621
B	HOH1332
B	EPU3450
B	GOL3471
B	LYS22

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 C 4461

Chain	Residue
C	LYS22
C	ARG120
C	ARG397
C	HOH1146
C	HOH1633
C	EPU4450
C	GOL4471

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 D 5461

Chain	Residue
D	LYS22
D	ARG120
D	HOH452
D	EPU5450
D	GOL5471

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 E 6461

Chain	Residue
E	LYS22
E	ARG120
E	ARG397
E	HOH583
E	HOH752
E	EPU6450
E	GOL6471

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 F 7461

Chain	Residue
F	LYS22
F	ARG120
F	HOH424
F	EPU7450
F	GOL7471

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 G 8461

Chain	Residue
G	LYS22
G	ARG120
G	ARG397
G	HOH436
G	HOH1037
G	EPU8450
G	GOL8471

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 G 8462

Chain	Residue
G	GLY114
G	SER115
G	ALA116
G	HOH438
H	MET366

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 H 9461

Chain	Residue
H	LYS22
H	ARG120
H	ARG397
H	HOH567
H	EPU9450
H	GOL9471

site_id	BC1
Number of Residues	31
Details	BINDING SITE FOR RESIDUE EPU E 6450

Chain	Residue
E	LYS22
E	ASN23
E	TRP95
E	ARG120
E	PRO121
E	VAL122
E	ASP123
E	LEU124
E	HIS125
E	LYS160
E	SER162
E	VAL163
E	GLY164
E	THR304
E	ASP305
E	ILE327
E	PHE328
E	ARG331
E	ARG371
E	HOH424
E	HOH425
E	HOH431
E	HOH433
E	HOH436
E	HOH438
E	HOH465
E	HOH596
E	HOH756
E	HOH798
E	PO46461
E	GOL6471

site_id	BC2
Number of Residues	32
Details	BINDING SITE FOR RESIDUE EPU B 3450

Chain	Residue
B	GLY164
B	THR304
B	ASP305
B	ILE327
B	PHE328
B	ARG331
B	ARG371
B	HOH422
B	HOH430
B	HOH431
B	HOH434
B	HOH445
B	HOH451
B	HOH452
B	HOH458
B	HOH472
B	HOH658
B	HOH917
B	HOH1438
B	PO43461
B	GOL3471
B	LYS22
B	ASN23
B	TRP95
B	ARG120
B	PRO121
B	VAL122
B	ASP123
B	LEU124
B	LYS160
B	SER162
B	VAL163

site_id	BC3
Number of Residues	30
Details	BINDING SITE FOR RESIDUE EPU C 4450

Chain	Residue
C	LYS22
C	ASN23
C	TRP95
C	ARG120
C	PRO121
C	VAL122
C	ASP123
C	LEU124
C	HIS125
C	LYS160
C	SER162
C	VAL163
C	GLY164
C	THR304
C	ASP305
C	ILE327
C	PHE328
C	ARG331
C	ARG371
C	HOH420
C	HOH421
C	HOH424
C	HOH425
C	HOH433
C	HOH445
C	HOH459
C	HOH522
C	HOH592
C	PO44461
C	GOL4471

site_id	BC4
Number of Residues	32
Details	BINDING SITE FOR RESIDUE EPU D 5450

Chain	Residue
D	LYS22
D	ASN23
D	TRP95
D	ARG120
D	PRO121
D	VAL122
D	ASP123
D	LEU124
D	HIS125
D	LYS160
D	SER162
D	VAL163
D	GLY164
D	THR304
D	ASP305
D	ILE327
D	PHE328
D	ARG331
D	ARG371
D	HOH427
D	HOH438
D	HOH444
D	HOH448
D	HOH451
D	HOH459
D	HOH464
D	HOH473
D	HOH641
D	HOH703
D	HOH1114
D	PO45461
D	GOL5471

site_id	BC5
Number of Residues	32
Details	BINDING SITE FOR RESIDUE EPU A 2450

Chain	Residue
A	LYS22
A	ASN23
A	TRP95
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	ARG331
A	ARG371
A	HOH422
A	HOH425
A	HOH429
A	HOH432
A	HOH439
A	HOH454
A	HOH462
A	HOH465
A	HOH667
A	HOH1742
A	HOH1766
A	PO42461
A	GOL2471

site_id	BC6
Number of Residues	30
Details	BINDING SITE FOR RESIDUE EPU F 7450

Chain	Residue
F	LYS22
F	ASN23
F	TRP95
F	ARG120
F	PRO121
F	VAL122
F	ASP123
F	LEU124
F	HIS125
F	LYS160
F	SER162
F	VAL163
F	GLY164
F	THR304
F	ASP305
F	ILE327
F	PHE328
F	ARG331
F	ARG371
F	HOH420
F	HOH427
F	HOH429
F	HOH447
F	HOH465
F	HOH580
F	HOH912
F	HOH1101
F	HOH1171
F	PO47461
F	GOL7471

site_id	BC7
Number of Residues	31
Details	BINDING SITE FOR RESIDUE EPU G 8450

Chain	Residue
G	LYS22
G	ASN23
G	TRP95
G	ARG120
G	PRO121
G	VAL122
G	ASP123
G	LEU124
G	HIS125
G	LYS160
G	SER162
G	VAL163
G	GLY164
G	THR304
G	ASP305
G	ILE327
G	PHE328
G	ARG331
G	ARG371
G	HOH420
G	HOH425
G	HOH426
G	HOH462
G	HOH476
G	HOH481
G	HOH485
G	HOH492
G	HOH532
G	HOH1354
G	PO48461
G	GOL8471

site_id	BC8
Number of Residues	31
Details	BINDING SITE FOR RESIDUE EPU H 9450

Chain	Residue
H	LYS22
H	ASN23
H	TRP95
H	ARG120
H	PRO121
H	VAL122
H	ASP123
H	LEU124
H	HIS125
H	LYS160
H	SER162
H	VAL163
H	GLY164
H	THR304
H	ASP305
H	ILE327
H	PHE328
H	ARG331
H	ARG371
H	HOH434
H	HOH440
H	HOH443
H	HOH446
H	HOH447
H	HOH461
H	HOH467
H	HOH472
H	HOH509
H	HOH934
H	PO49461
H	GOL9471

site_id	BC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 2471

Chain	Residue
A	ARG91
A	ALA92
A	ILE94
A	TRP95
A	HIS125
A	GLY164
A	HOH429
A	EPU2450
A	PO42461

site_id	CC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 2472

Chain	Residue
A	ARG252
A	TRP279
A	HOH1610

site_id	CC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL C 2473

Chain	Residue
A	TYR393
C	ARG391

site_id	CC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL B 3471

Chain	Residue
B	ARG91
B	ALA92
B	TRP95
B	HIS125
B	GLY164
B	HOH430
B	HOH621
B	EPU3450
B	PO43461

site_id	CC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GOL B 3472

Chain	Residue
B	ARG252

site_id	CC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL C 3473

Chain	Residue
A	ARG391
C	TYR393

site_id	CC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL C 4471

Chain	Residue
C	ARG91
C	ILE94
C	TRP95
C	ARG120
C	HIS125
C	HOH420
C	EPU4450
C	PO44461

site_id	CC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL C 4472

Chain	Residue
C	ARG252
C	HOH1648

site_id	CC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL C 4474

Chain	Residue
A	GLU329
A	HOH1435
C	GLU325
C	PHE328
C	GLU329
C	ASN330
C	ARG331
C	PHE332
C	HOH625

site_id	CC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL D 5471

Chain	Residue
D	ARG91
D	ALA92
D	ILE94
D	ARG120
D	HIS125
D	GLY164
D	HOH427
D	EPU5450
D	PO45461

site_id	DC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL D 5472

Chain	Residue
D	VAL250
D	ARG252
D	HOH1290

site_id	DC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL E 6471

Chain	Residue
E	ARG91
E	ALA92
E	ILE94
E	TRP95
E	HIS125
E	GLY164
E	HOH425
E	EPU6450
E	PO46461

site_id	DC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL F 7471

Chain	Residue
F	ARG91
F	ALA92
F	ILE94
F	TRP95
F	ARG120
F	HIS125
F	GLY164
F	HOH447
F	EPU7450
F	PO47461

site_id	DC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL G 8471

Chain	Residue
G	ARG91
G	ALA92
G	TRP95
G	HIS125
G	GLY164
G	HOH420
G	EPU8450
G	PO48461

site_id	DC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GOL E 8472

Chain	Residue
E	ARG252

site_id	DC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL H 9471

Chain	Residue
H	ARG91
H	ILE94
H	TRP95
H	ARG120
H	HIS125
H	GLY164
H	EPU9450
H	PO49461

site_id	DC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL H 9472

Chain	Residue
H	VAL250
H	ARG252
H	TRP279

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Proton donor => ECO:0000269\|PubMed:20392080, ECO:0000269\|PubMed:22378791, ECO:0007744\|PDB:3LTH

Chain	Residue	Details
A	SER115
B	SER115
C	SER115
D	SER115
E	SER115
F	SER115
G	SER115
H	SER115

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000305\|PubMed:22378791, ECO:0007744\|PDB:3SWQ

Chain	Residue	Details
A	LYS22
B	LYS22
C	LYS22
D	LYS22
E	LYS22
F	LYS22
G	LYS22
H	LYS22

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00111

Chain	Residue	Details
A	ARG91
B	ARG91
C	ARG91
D	ARG91
E	ARG91
F	ARG91
G	ARG91
H	ARG91

site_id	SWS_FT_FI4
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:20392080, ECO:0000269\|PubMed:22378791, ECO:0007744\|PDB:3LTH, ECO:0007744\|PDB:3SWQ

Chain	Residue	Details
C	ILE327
D	ARG120
D	ASP305
D	ILE327
E	ARG120
E	ASP305
E	ILE327
F	ARG120
F	ASP305
F	ILE327
G	ARG120
G	ASP305
G	ILE327
H	ARG120
H	ASP305
H	ILE327
A	ARG120
A	ASP305
A	ILE327
B	ARG120
B	ASP305
B	ILE327
C	ARG120
C	ASP305

site_id	SWS_FT_FI5
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:22378791, ECO:0007744\|PDB:3SWQ

Chain	Residue	Details
A	LYS160
B	LYS160
C	LYS160
D	LYS160
E	LYS160
F	LYS160
G	LYS160
H	LYS160

site_id	SWS_FT_FI6
Number of Residues	8
Details	MOD_RES: 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000269\|PubMed:22378791

Chain	Residue	Details
A	SER115
B	SER115
C	SER115
D	SER115
E	SER115
F	SER115
G	SER115
H	SER115

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	SER115	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	SER115	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	SER115	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	SER115	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

site_id	MCSA5
Number of Residues	6
Details	M-CSA 369

Chain	Residue	Details
E	LYS22	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor
E	ASN23	electrostatic stabiliser, hydrogen bond donor
E	SER115	activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay
E	ARG120	electrostatic stabiliser, proton acceptor, proton donor
E	ASP305	activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
E	ARG397	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA6
Number of Residues	6
Details	M-CSA 369

Chain	Residue	Details
F	LYS22	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor
F	ASN23	electrostatic stabiliser, hydrogen bond donor
F	SER115	activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay
F	ARG120	electrostatic stabiliser, proton acceptor, proton donor
F	ASP305	activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
F	ARG397	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA7
Number of Residues	6
Details	M-CSA 369

Chain	Residue	Details
G	LYS22	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor
G	ASN23	electrostatic stabiliser, hydrogen bond donor
G	SER115	activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay
G	ARG120	electrostatic stabiliser, proton acceptor, proton donor
G	ASP305	activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
G	ARG397	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA8
Number of Residues	6
Details	M-CSA 369

Chain	Residue	Details
H	LYS22	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor
H	ASN23	electrostatic stabiliser, hydrogen bond donor
H	SER115	activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay
H	ARG120	electrostatic stabiliser, proton acceptor, proton donor
H	ASP305	activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
H	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)