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4Y96

Crystal structure of Triosephosphate Isomerase from Gemmata obscuriglobus

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
B0004807molecular_functiontriose-phosphate isomerase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016853molecular_functionisomerase activity
B0019563biological_processglycerol catabolic process
B0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue NA A 301
ChainResidue
AASN14
ALYS16
AHIS99
AHOH530
AHOH637

site_idAC2
Number of Residues10
Detailsbinding site for residue PO4 A 303
ChainResidue
AGLY238
AGLY239
AHOH402
AHOH506
AHOH529
AHOH530
AALA175
AILE176
AGLY177
ASER217

site_idAC3
Number of Residues2
Detailsbinding site for residue CA A 304
ChainResidue
AASP204
ALYS205

site_idAC4
Number of Residues5
Detailsbinding site for residue NA B 301
ChainResidue
BASN14
BLYS16
BHIS99
BGLU171
BHOH622

site_idAC5
Number of Residues11
Detailsbinding site for residue PO4 B 302
ChainResidue
BALA175
BILE176
BGLY177
BSER217
BGLY238
BGLY239
BHOH409
BHOH516
BHOH518
BHOH537
BHOH622

Functional Information from PROSITE/UniProt
site_idPS00171
Number of Residues11
DetailsTIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG
ChainResidueDetails
AALA169-GLY179

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PDB entries from 2024-11-13

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