Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1S89

H98N Mutant of Methylglyoxal Synthase from E. coli complexed with Phosphoglycolic Acid

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
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0008929	molecular_function	methylglyoxal synthase activity
D	0016829	molecular_function	lyase activity
D	0019242	biological_process	methylglyoxal biosynthetic process
D	0034214	biological_process	protein hexamerization
D	0042802	molecular_function	identical protein binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0008929	molecular_function	methylglyoxal synthase activity
E	0016829	molecular_function	lyase activity
E	0019242	biological_process	methylglyoxal biosynthetic process
E	0034214	biological_process	protein hexamerization
E	0042802	molecular_function	identical protein binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0008929	molecular_function	methylglyoxal synthase activity
F	0016829	molecular_function	lyase activity
F	0019242	biological_process	methylglyoxal biosynthetic process
F	0034214	biological_process	protein hexamerization
F	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PGA A 201

Chain	Residue
A	VAL17
A	PRO67
A	ASP71
A	ASN98
A	HOH215
F	ARG150
A	ALA18
A	HIS19
A	LYS23
A	THR45
A	THR47
A	THR48
A	SER65
A	GLY66

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PGA B 202

Chain	Residue
B	VAL17
B	ALA18
B	HIS19
B	LYS23
B	THR45
B	THR47
B	THR48
B	SER65
B	GLY66
B	PRO67
B	ASP71
B	ASN98
B	HOH217
E	ARG150

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PGA C 203

Chain	Residue
C	VAL17
C	ALA18
C	HIS19
C	LYS23
C	THR45
C	THR47
C	THR48
C	SER65
C	GLY66
C	ASP71
C	ASN98
C	HOH224
D	ARG150

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PGA D 204

Chain	Residue
C	ARG150
D	VAL17
D	ALA18
D	HIS19
D	LYS23
D	THR45
D	THR47
D	THR48
D	SER65
D	GLY66
D	PRO67
D	ASP71
D	ASN98
D	HOH212

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PGA E 205

Chain	Residue
B	ARG150
E	VAL17
E	ALA18
E	LYS23
E	THR45
E	THR47
E	THR48
E	SER65
E	GLY66
E	PRO67
E	ASP71
E	ASN98
E	HOH210

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PGA F 206

Chain	Residue
A	ARG150
F	VAL17
F	ALA18
F	LYS23
F	THR45
F	THR47
F	THR48
F	SER65
F	GLY66
F	PRO67
F	ASP71
F	ASN98
F	HOH218

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	876
Details	Domain: {"description":"MGS-like","evidences":[{"source":"HAMAP-Rule","id":"MF_00549","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
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_FI3
Number of Residues	6
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_FI4
Number of Residues	30
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_FI5
Number of Residues	6
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	Annotated By Reference To The Literature 1b93

Chain	Residue	Details
A	ASN98
A	ASP71
A	HIS19
A	ASP101
A	ASP91
A	GLY66

site_id	CSA2
Number of Residues	6
Details	Annotated By Reference To The Literature 1b93

Chain	Residue	Details
B	ASN98
B	ASP71
B	HIS19
B	ASP101
B	ASP91
B	GLY66

site_id	CSA3
Number of Residues	6
Details	Annotated By Reference To The Literature 1b93

Chain	Residue	Details
C	ASN98
C	ASP71
C	HIS19
C	ASP101
C	ASP91
C	GLY66

site_id	CSA4
Number of Residues	6
Details	Annotated By Reference To The Literature 1b93

Chain	Residue	Details
D	ASN98
D	ASP71
D	HIS19
D	ASP101
D	ASP91
D	GLY66

site_id	CSA5
Number of Residues	6
Details	Annotated By Reference To The Literature 1b93

Chain	Residue	Details
E	ASN98
E	ASP71
E	HIS19
E	ASP101
E	ASP91
E	GLY66

site_id	CSA6
Number of Residues	6
Details	Annotated By Reference To The Literature 1b93

Chain	Residue	Details
F	ASN98
F	ASP71
F	HIS19
F	ASP101
F	ASP91
F	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	ASN98	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	ASN98	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	ASN98	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

site_id	MCSA4
Number of Residues	7
Details	M-CSA 85

Chain	Residue	Details
D	HIS19	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	GLY66	electrostatic stabiliser, hydrogen bond donor, steric role
D	ASP71	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	ASP91	activator, electrostatic stabiliser, hydrogen bond acceptor
D	ASN98	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	ASP101	activator, electrostatic stabiliser, hydrogen bond acceptor, repulsive charge-charge interaction
D	ARG107	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA5
Number of Residues	7
Details	M-CSA 85

Chain	Residue	Details
E	HIS19	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
E	GLY66	electrostatic stabiliser, hydrogen bond donor, steric role
E	ASP71	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
E	ASP91	activator, electrostatic stabiliser, hydrogen bond acceptor
E	ASN98	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
E	ASP101	activator, electrostatic stabiliser, hydrogen bond acceptor, repulsive charge-charge interaction
E	ARG107	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA6
Number of Residues	7
Details	M-CSA 85

Chain	Residue	Details
F	HIS19	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
F	GLY66	electrostatic stabiliser, hydrogen bond donor, steric role
F	ASP71	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
F	ASP91	activator, electrostatic stabiliser, hydrogen bond acceptor
F	ASN98	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
F	ASP101	activator, electrostatic stabiliser, hydrogen bond acceptor, repulsive charge-charge interaction
F	ARG107	electrostatic stabiliser, hydrogen bond donor

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