Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3KQA

MurA dead-end complex with terreic acid

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	14
Details	BINDING SITE FOR RESIDUE TR9 A 500

Chain	Residue
A	CYS115
A	HOH470
A	HOH502
A	HOH514
B	GLU130
B	HOH429
A	ALA116
A	LEU138
A	CA420
A	CA421
A	HOH450
A	HOH451
A	HOH457
A	HOH464

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE TR9 B 500

Chain	Residue
A	GLU130
B	CYS115
B	ALA116
B	LYS137
B	LEU138
B	CA421
B	CA422
B	HOH458
B	HOH466
B	HOH503
B	HOH524
B	HOH531

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TR9 C 500

Chain	Residue
C	CYS115
C	ALA116
C	LEU138
C	CA420
C	CA421
C	HOH489
D	PHE127
D	GLU130

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TR9 D 500

Chain	Residue
C	ILE126
C	PHE127
C	GLU130
D	CYS115
D	ALA116
D	LEU138
D	CA420
D	CA421

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 420

Chain	Residue
A	LEU138
A	HOH451
A	HOH457
A	TR9500

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 421

Chain	Residue
A	ALA116
A	HOH446
A	HOH464
A	HOH470
A	TR9500
A	HOH502

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 420

Chain	Residue
A	ILE136
B	ILE136
B	HOH465
B	HOH483
B	HOH520

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 421

Chain	Residue
B	LEU138
B	HOH466
B	TR9500
B	HOH524
B	HOH542

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA B 422

Chain	Residue
B	ALA116
B	HOH425
B	HOH476
B	HOH490
B	TR9500
B	HOH503
B	HOH531

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 423

Chain	Residue
B	PHE104
B	GLN106
B	HOH528
B	HOH575
C	ASN148

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA C 420

Chain	Residue
C	ALA116
C	HOH489
C	TR9500

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA C 421

Chain	Residue
C	LEU138
C	TR9500
D	GLU130

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA D 420

Chain	Residue
C	GLU130
D	LEU138
D	HOH434
D	TR9500

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA D 421

Chain	Residue
D	ALA116
D	HOH460
D	TR9500

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)