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4MKN

Crystal structure of chloroplastic triosephosphate isomerase from Chlamydomonas reinhardtii at 1.1 A of resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004807molecular_functiontriose-phosphate isomerase activity
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 Residues8
DetailsBINDING SITE FOR RESIDUE MRD A 301
ChainResidue
ALYS13
ASER213
AGLY234
AGLY235
AHOH465
AHOH473
AHOH559
AHOH638

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MRD A 302
ChainResidue
ALEU101
APHE102
AVAL108
AHOH452
ATRP67

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MPD A 303
ChainResidue
AGLY137
ASER138
AVAL139
APHE140
AMRD304
AHOH440
AHOH468
AHOH589
AHOH633

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MRD A 304
ChainResidue
AARG134
APHE140
AGLU185
AMPD303

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MRD A 305
ChainResidue
ASER105
AASN106
AGLU107
AHOH487
AHOH571
AHOH572

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MRD A 306
ChainResidue
ALEU131
AARG134
ATRP170
ATRP170
AGLN182
AGLN182
AHOH426
AHOH426
AHOH438
AHOH438

Functional Information from PROSITE/UniProt
site_idPS00171
Number of Residues11
DetailsTIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG
ChainResidueDetails
AALA165-GLY175

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PDB entries from 2024-11-06

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