Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4Y9A

Crystal structure of Triosephosphate Isomerase from Streptomyces coelicolor

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
C0004807molecular_functiontriose-phosphate isomerase activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006094biological_processgluconeogenesis
C0006096biological_processglycolytic process
C0016853molecular_functionisomerase activity
C0019563biological_processglycerol catabolic process
C0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
D0004807molecular_functiontriose-phosphate isomerase activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006094biological_processgluconeogenesis
D0006096biological_processglycolytic process
D0016853molecular_functionisomerase activity
D0019563biological_processglycerol catabolic process
D0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00171
Number of Residues11
DetailsTIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG
ChainResidueDetails
AALA174-GLY184

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Electrophile => ECO:0000255|HAMAP-Rule:MF_00147
ChainResidueDetails
AHIS104
BHIS104
CHIS104
DHIS104

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00147
ChainResidueDetails
AGLU176
BGLU176
CGLU176
DGLU176

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00147
ChainResidueDetails
AASN14
CGLY182
CSER222
CGLY243
DASN14
DGLY182
DSER222
DGLY243
AGLY182
ASER222
AGLY243
BASN14
BGLY182
BSER222
BGLY243
CASN14

220113

PDB entries from 2024-05-22

PDB statisticsPDBj update infoContact PDBjnumon