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1VMD

Crystal structure of Methylglyoxal synthase (TM1185) from Thermotoga maritima at 2.06 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0008929molecular_functionmethylglyoxal synthase activity
A0016829molecular_functionlyase activity
A0019242biological_processmethylglyoxal biosynthetic process
B0005829cellular_componentcytosol
B0008929molecular_functionmethylglyoxal synthase activity
B0016829molecular_functionlyase activity
B0019242biological_processmethylglyoxal biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 167
ChainResidue
ALYS27
BILE155
ATHR49
ATHR51
ATHR52
ASER69
AGLY70
AHOH174
AHOH189
AHOH204

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 167
ChainResidue
BLYS27
BTHR49
BTHR51
BTHR52
BSER69
BGLY70
BHOH187

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 168
ChainResidue
AASN117
BARG26
BARG124

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 168
ChainResidue
AARG26
AARG124
BHOH181

Functional Information from PROSITE/UniProt
site_idPS01335
Number of Residues9
DetailsMETHYLGLYOXAL_SYNTH Methylglyoxal synthase active site. SGPLGGDqQ
ChainResidueDetails
ASER69-GLN77

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00549
ChainResidueDetails
AASP75
BASP75

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00549
ChainResidueDetails
AHIS23
BHIS102
ALYS27
ATHR49
ASER69
AHIS102
BHIS23
BLYS27
BTHR49
BSER69

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1b93
ChainResidueDetails
AHIS102
AASP75
AASP95
AASP105
AHIS23
AGLY70

site_idCSA2
Number of Residues6
DetailsAnnotated By Reference To The Literature 1b93
ChainResidueDetails
BHIS102
BASP75
BASP95
BASP105
BHIS23
BGLY70

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PDB entries from 2024-07-31

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