Structure of PDB 1itz Chain B

Receptor sequence
>1itzB (length=666) Species: 4577 (Zea mays) [Search protein sequence]
AATGELLEKSVNTIRFLAIDAVEKANSGHPGLPMGCAPMGHVLYDEVMRY
NPKNPYWFNRDRFVLSAGHGCMLQYALLHLAGYDSVKEEDLKQFRQWGSR
TPGHPENFETPGVEVTTGPLGQGIANAVGLALAEKHLAARFNKPDSEIVD
HYTYVILGDGCQMEGIANEACSLAGHWGLGKLIAFYDDNHISIDGDTEIA
FTEDVSTRFEALGWHTIWVKNGNTGYDDIRAAIKEAKAVTDKPTLIKVTT
TIGFGSPNKANSYSVHGSALGAKEVEATRQNLGWPYDTFFVPEDVKSHWS
RHTPEGAALEADWNAKFAEYEKKYADDAATLKSIITGELPTGWVDALPKY
TPESPGDATRNLSQQCLNALANVVPGLIGGSADLASSNMTLLKMFGDFQK
DTAEERNVRFGVREHGMGAICNGIALHSPGFVPYCATFFVFTDYMRGAMR
ISALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLVSFRAMPNILMLRPADG
NETAGAYKVAVLNRKRPSILALSRQKLPHLPGTSIEGVEKGGYTISDNST
GNKPDLIVMGTGSELEIAAKAADELRKEGKTVRVVSFVSWELFDEQSDEY
KESVLPAAVTARISIEAGSTLGWQKYVGAQGKAIGIDKFGASAPAGTIYK
EYGITVESIIAAAKSF
3D structure
PDB1itz Structure and properties of an engineered transketolase from maize
ChainB
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H38 I261 H275 E423 H486
Catalytic site (residue number reindexed from 1) H29 I252 H266 E414 H477
Enzyme Commision number 2.2.1.1: transketolase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 TPP B D392 E423 F450 Y453 D383 E414 F441 Y444
BS02 MG B D168 N198 I200 D159 N189 I191
BS03 TPP B H78 L129 D168 G169 N198 I200 I202 I261 H275 H69 L120 D159 G160 N189 I191 I193 I252 H266
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004802 transketolase activity
GO:0005509 calcium ion binding
GO:0016740 transferase activity
GO:0030145 manganese ion binding
GO:0046872 metal ion binding
GO:0050897 cobalt ion binding
Biological Process
GO:0006098 pentose-phosphate shunt
GO:0019253 reductive pentose-phosphate cycle
Cellular Component
GO:0005829 cytosol
GO:0009507 chloroplast
GO:0009535 chloroplast thylakoid membrane
GO:0009579 thylakoid
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1itz, PDBe:1itz, PDBj:1itz
PDBsum1itz
PubMed12913150
UniProtQ7SIC9|TKTC_MAIZE Transketolase, chloroplastic

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