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4Y8F

Crystal structure of Triosephosphate Isomerase from Clostridium perfringens

Functional Information from GO Data
ChainGOidnamespacecontents
A0004807molecular_functiontriose-phosphate isomerase activity
A0005737cellular_componentcytoplasm
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue ACT A 301
ChainResidue
AHIS16
ATYR17
ALYS73
AARG83
AHOH404
AHOH427

site_idAC2
Number of Residues4
Detailsbinding site for residue ACT A 302
ChainResidue
AHOH416
AGLU154
AGLY155
ALEU156

site_idAC3
Number of Residues5
Detailsbinding site for residue NA A 303
ChainResidue
AMET225
ALYS227
AILE230
AHOH517
AHOH767

site_idAC4
Number of Residues4
Detailsbinding site for residue NA A 304
ChainResidue
AGLN184
AGLU187
AHOH601
AHOH672

site_idAC5
Number of Residues3
Detailsbinding site for residue NA A 305
ChainResidue
ATHR179
ASER215
AGLN224

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Electrophile => ECO:0000255|HAMAP-Rule:MF_00147
ChainResidueDetails
AHIS97

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00147
ChainResidueDetails
AGLU169

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00147
ChainResidueDetails
AASN12
AGLY175
ASER215
AGLY236

223166

PDB entries from 2024-07-31

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