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4BI7

CRYSTAL STRUCTURE OF A MUTANT (C202A) OF TRIOSEPHOSPHATE ISOMERASE FROM GIARDIA LAMBLIA COMPLEXED WITH 2-PHOSPHOGLYCOLIC ACID

Replaces:  2YC7
Functional Information from GO Data
ChainGOidnamespacecontents
A0004807molecular_functiontriose-phosphate isomerase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0008929molecular_functionmethylglyoxal synthase activity
A0016829molecular_functionlyase activity
A0016853molecular_functionisomerase activity
A0019563biological_processglycerol catabolic process
A0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PGA A 401
ChainResidue
AASN11
AGLY238
AHOH2013
AHOH2172
AHOH2174
ALYS13
AHIS96
AGLU170
ASER174
AILE175
AGLY176
ASER216
AGLY237

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 1258
ChainResidue
AILE52
AASN55
ALEU60
AARG61
AILE62
AHOH2055
AHOH2069
AHOH2107
AHOH2192

Functional Information from PROSITE/UniProt
site_idPS00171
Number of Residues11
DetailsTIM_1 Triosephosphate isomerase active site. AYEPVWSIGTG
ChainResidueDetails
AALA168-GLY178

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Electrophile => ECO:0000255|PROSITE-ProRule:PRU10127
ChainResidueDetails
AHIS96

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10127
ChainResidueDetails
AGLU170

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10127
ChainResidueDetails
AASN11
ALYS13

221051

PDB entries from 2024-06-12

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