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4X22

Crystal structure of Leptospira Interrogans Triosephosphate Isomerase (LiTIM)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004807molecular_functiontriose-phosphate isomerase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0019563biological_processglycerol catabolic process
A0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue EDO A 301
ChainResidue
AHOH417

site_idAC2
Number of Residues3
Detailsbinding site for residue EDO A 302
ChainResidue
AASN14
AALA74
AALA75

site_idAC3
Number of Residues3
Detailsbinding site for residue EDO A 303
ChainResidue
ASER147
AARG150
AGLU151

site_idAC4
Number of Residues3
Detailsbinding site for residue EDO A 304
ChainResidue
AHOH427
ASER183
AGLU229

site_idAC5
Number of Residues3
Detailsbinding site for residue PG0 A 305
ChainResidue
ALEU104
ALEU104
APHE110

Functional Information from PROSITE/UniProt
site_idPS00171
Number of Residues11
DetailsTIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG
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
AASN10
AGLY175
ASER217
AGLY238

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PDB entries from 2025-06-11

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