Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1B93

METHYLGLYOXAL SYNTHASE FROM ESCHERICHIA COLI

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0008929	molecular_function	methylglyoxal synthase activity
A	0016829	molecular_function	lyase activity
A	0019242	biological_process	methylglyoxal biosynthetic process
A	0034214	biological_process	protein hexamerization
A	0042802	molecular_function	identical protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0008929	molecular_function	methylglyoxal synthase activity
B	0016829	molecular_function	lyase activity
B	0019242	biological_process	methylglyoxal biosynthetic process
B	0034214	biological_process	protein hexamerization
B	0042802	molecular_function	identical protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0008929	molecular_function	methylglyoxal synthase activity
C	0016829	molecular_function	lyase activity
C	0019242	biological_process	methylglyoxal biosynthetic process
C	0034214	biological_process	protein hexamerization
C	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 B 301

Chain	Residue
B	LYS23
B	THR45
B	THR47
B	THR48
B	SER65
B	GLY66
B	ARG150
B	FMT204
B	HOH472

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT A 201

Chain	Residue
A	HIS19
A	GLY66
A	ASP71
A	PHE88
A	HIS98
A	FMT202

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT A 202

Chain	Residue
A	ALA18
A	THR45
A	SER65
A	GLY66
A	FMT201
A	FMT203

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT A 203

Chain	Residue
A	LEU16
A	VAL17
A	ALA18
A	LYS23
A	THR45
A	THR48
A	FMT202

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT B 204

Chain	Residue
B	VAL17
B	HIS19
B	ASP71
B	PHE88
B	HIS98
B	PO4301

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FMT C 205

Chain	Residue
C	VAL17
C	HIS19
C	GLY66
C	ASP71
C	PHE88
C	HIS98
C	FMT206
C	HOH518

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT C 206

Chain	Residue
C	LYS23
C	THR45
C	SER65
C	GLY66
C	FMT205
C	FMT207
C	HOH540

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT C 207

Chain	Residue
C	LEU16
C	VAL17
C	ALA18
C	LYS23
C	THR45
C	THR48
C	FMT206

Functional Information from PROSITE/UniProt

site_id	PS01335
Number of Residues	9
Details	METHYLGLYOXAL_SYNTH Methylglyoxal synthase active site. SGPMGGDqQ

Chain	Residue	Details
A	SER65-GLN73

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00549","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10715115","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11389594","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15049687","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9665712","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00549","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11389594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IK4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	15
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00549","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10715115","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11389594","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15049687","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EGH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1IK4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1S89","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1S8A","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00549","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10715115","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11389594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EGH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1IK4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	6
Details	a catalytic site defined by CSA, PubMed 10715115, 10368300

Chain	Residue	Details
A	HIS98
A	ASP71
A	HIS19
A	ASP101
A	ASP91
A	GLY66

site_id	CSA2
Number of Residues	6
Details	a catalytic site defined by CSA, PubMed 10715115, 10368300

Chain	Residue	Details
B	HIS98
B	ASP71
B	HIS19
B	ASP101
B	ASP91
B	GLY66

site_id	CSA3
Number of Residues	6
Details	a catalytic site defined by CSA, PubMed 10715115, 10368300

Chain	Residue	Details
C	HIS98
C	ASP71
C	HIS19
C	ASP101
C	ASP91
C	GLY66

site_id	MCSA1
Number of Residues	7
Details	M-CSA 85

Chain	Residue	Details
A	HIS19	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	GLY66	electrostatic stabiliser, hydrogen bond donor, steric role
A	ASP71	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ASP91	activator, electrostatic stabiliser, hydrogen bond acceptor
A	HIS98	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ASP101	activator, electrostatic stabiliser, hydrogen bond acceptor, repulsive charge-charge interaction
A	ARG107	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA2
Number of Residues	7
Details	M-CSA 85

Chain	Residue	Details
B	HIS19	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	GLY66	electrostatic stabiliser, hydrogen bond donor, steric role
B	ASP71	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	ASP91	activator, electrostatic stabiliser, hydrogen bond acceptor
B	HIS98	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	ASP101	activator, electrostatic stabiliser, hydrogen bond acceptor, repulsive charge-charge interaction
B	ARG107	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA3
Number of Residues	7
Details	M-CSA 85

Chain	Residue	Details
C	HIS19	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	GLY66	electrostatic stabiliser, hydrogen bond donor, steric role
C	ASP71	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	ASP91	activator, electrostatic stabiliser, hydrogen bond acceptor
C	HIS98	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	ASP101	activator, electrostatic stabiliser, hydrogen bond acceptor, repulsive charge-charge interaction
C	ARG107	electrostatic stabiliser, hydrogen bond donor

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