Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1EGH

STRUCTURE OF METHYLGLYOXAL SYNTHASE COMPLEXED WITH THE COMPETITIVE INHIBITOR 2-PHOSPHOGLYCOLATE

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	ASP71
A	HIS98
A	HOH381
A	HOH482
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 211

Chain	Residue
B	VAL17
B	ALA18
B	LYS23
B	THR45
B	THR47
B	THR48
B	SER65
B	GLY66
B	PRO67
B	ASP71
B	HIS98
B	HOH367
B	HOH527
E	ARG150

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PGA C 221

Chain	Residue
C	VAL17
C	ALA18
C	HIS19
C	LYS23
C	THR45
C	THR47
C	THR48
C	SER65
C	GLY66
C	ASP71
C	HIS98
C	HOH353
D	ARG150

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PGA D 231

Chain	Residue
C	ARG150
D	VAL17
D	ALA18
D	HIS19
D	LYS23
D	THR45
D	THR47
D	THR48
D	SER65
D	GLY66
D	ASP71
D	HIS98
D	HOH339
D	HOH533

site_id	AC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PGA E 241

Chain	Residue
B	ARG150
E	VAL17
E	ALA18
E	HIS19
E	LYS23
E	THR45
E	THR47
E	THR48
E	SER65
E	GLY66
E	ASP71
E	HIS98
E	HOH326
E	HOH529

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PGA F 251

Chain	Residue
A	ARG150
F	VAL17
F	ALA18
F	LYS23
F	THR45
F	THR47
F	THR48
F	SER65
F	GLY66
F	ASP71
F	HIS98
F	HOH312

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	584
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	HIS98
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	HIS98
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	HIS98
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	HIS98
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	HIS98
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	HIS98
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	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

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	HIS98	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	HIS98	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	HIS98	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)