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1SSG

Understanding protein lids: Structural analysis of active hinge mutants in triosephosphate isomerase

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 Residues12
DetailsBINDING SITE FOR RESIDUE PGA A 300
ChainResidue
AASN11
AGLY232
AGLY233
AHOH351
ALYS13
AHIS95
AGLU165
AALA169
AILE170
AGLY171
AGLY210
ASER211

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PGA B 1300
ChainResidue
BASN11
BLYS13
BHIS95
BGLU165
BALA169
BILE170
BGLY171
BSER211
BLEU230
BGLY232
BGLY233
BHOH1312
BHOH1337

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 1301
ChainResidue
BHIS100
BLYS130

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 1302
ChainResidue
ALYS5
BASP56
BALA57

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
ATHR213

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
AARG99
AHIS100
ALYS130

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1
ChainResidue
APHE50
AGLN53
AHOH340
BASP49
BPHE50
BGLN53

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 1303
ChainResidue
BLYS68
BALA114
BHIS115
BALA118

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 1304
ChainResidue
BSER197
BASP198
BHOH1343

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
ASER96
BSER96

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_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1hti
ChainResidueDetails
ALYS13
AHIS95
AASN11
AGLU165
AGLY171

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1hti
ChainResidueDetails
BLYS13
BHIS95
BASN11
BGLU165
BGLY171

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
ASER96activator, 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
BSER96activator, 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 2024-05-01

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