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3KXQ

Crystal structure of triosephosphate isomerase from bartonella henselae at 1.6A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004807molecular_functiontriose-phosphate isomerase activity
A0005737cellular_componentcytoplasm
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
B0004807molecular_functiontriose-phosphate isomerase activity
B0005737cellular_componentcytoplasm
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016853molecular_functionisomerase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 A 310
ChainResidue
AASN12
ALYS14
AHIS99
ALEU233
AILE234
AGLY235
AHOH334
AHOH492

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NO3 B 310
ChainResidue
BLYS14
BHIS99
BLEU233
BILE234
BGLY235
BHOH256
BHOH391
BHOH457
BASN12

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 300
ChainResidue
AALA190
AHIS193
AHIS194

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 301
ChainResidue
AGLY80
AASP81
AARG102
BGLY80
BASP81
BARG102

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 302
ChainResidue
ATRP13
ALEU239
ALYS240
AHOH471
AHOH483

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 302
ChainResidue
BTRP13
BLEU239
BHOH405
BHOH421
BHOH479

Functional Information from PROSITE/UniProt
site_idPS00171
Number of Residues11
DetailsTIM_1 Triosephosphate isomerase active site. AYEPVWAVGTG
ChainResidueDetails
AALA167-GLY177

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Electrophile => ECO:0000255|HAMAP-Rule:MF_00147
ChainResidueDetails
AHIS99
BHIS99

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00147
ChainResidueDetails
AGLU169
BGLU169

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00147
ChainResidueDetails
AASN12
AGLY175
ASER214
AGLY235
BASN12
BGLY175
BSER214
BGLY235

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1hti
ChainResidueDetails
AGLU169
ALYS14
AHIS99
AASN12

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1hti
ChainResidueDetails
BGLU169
BLYS14
BHIS99
BASN12

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PDB entries from 2024-07-24

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