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1TPW

TRIOSEPHOSPHATE ISOMERASE DRINKS WATER TO KEEP HEALTHY

Functional Information from GO Data
ChainGOidnamespacecontents
A0004807molecular_functiontriose-phosphate isomerase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006006biological_processglucose metabolic process
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0008929molecular_functionmethylglyoxal synthase activity
A0016829molecular_functionlyase activity
A0016853molecular_functionisomerase activity
A0019242biological_processmethylglyoxal biosynthetic process
A0019563biological_processglycerol catabolic process
A0019682biological_processglyceraldehyde-3-phosphate metabolic process
A0031625molecular_functionubiquitin protein ligase binding
A0042803molecular_functionprotein homodimerization activity
A0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
A0061621biological_processcanonical glycolysis
B0004807molecular_functiontriose-phosphate isomerase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006006biological_processglucose metabolic process
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0008929molecular_functionmethylglyoxal synthase activity
B0016829molecular_functionlyase activity
B0016853molecular_functionisomerase activity
B0019242biological_processmethylglyoxal biosynthetic process
B0019563biological_processglycerol catabolic process
B0019682biological_processglyceraldehyde-3-phosphate metabolic process
B0031625molecular_functionubiquitin protein ligase binding
B0042803molecular_functionprotein homodimerization activity
B0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
B0061621biological_processcanonical glycolysis
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PGH A 250
ChainResidue
ALYS13
AHIS95
AGLU165
AALA169
AILE170
AGLY171
AGLY210
ASER211
ALEU230
AGLY232
AGLY233
AHOH648
AHOH673
AHOH726
AHOH777
AASN11

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PGH B 250
ChainResidue
BASN11
BLYS13
BHIS95
BGLU165
BALA169
BILE170
BGLY171
BGLY210
BSER211
BLEU230
BGLY232
BGLY233
BHOH692
BHOH710
BHOH800
BHOH856

site_idACA
Number of Residues4
Details
ChainResidue
AGLU165
AHIS95
APRO96
ALYS13

site_idACB
Number of Residues4
Details
ChainResidue
BGLU165
BHIS95
BPRO96
BLYS13

Functional Information from PROSITE/UniProt
site_idPS00171
Number of Residues11
DetailsTIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG
ChainResidueDetails
AALA163-GLY173

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Electrophile => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH
ChainResidueDetails
APRO96
BPRO96

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH
ChainResidueDetails
APRO166
BPRO166

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH
ChainResidueDetails
ATRP12
AMET14
BTRP12
BMET14

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 324
ChainResidueDetails
ATRP12electrostatic stabiliser
AMET14attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay
APRO96activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AARG98proton acceptor, proton donor, steric role
APRO166activator, proton acceptor, proton donor
ATHR172electrostatic stabiliser
AVAL212electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues7
DetailsM-CSA 324
ChainResidueDetails
BTRP12electrostatic stabiliser
BMET14attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay
BPRO96activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BARG98proton acceptor, proton donor, steric role
BPRO166activator, proton acceptor, proton donor
BTHR172electrostatic stabiliser
BVAL212electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-04-24

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