Structure of PDB 4okd Chain B

Receptor sequence
>4okdB (length=792) Species: 3055 (Chlamydomonas reinhardtii) [Search protein sequence]
FCEPSGQPASTAYGPALTGRPAPLGASIDADTGAINFSVFSSSAESVSLV
LFTEADLNAGRATFEIPLDPYVNRTGDVWHIMLPDLRDDLLYGYRVEGVH
QEEDKDYPGMRHDKRRVVLDPYAVAVLNRRRWGQMGPNLPYGEEGVLGVM
PTWPQAAAALPAASAFDWEGDTPLNLPMESLVIYEAHVRGFTAHASSGVA
APGTYAGMVERLDYLKSLGVNAIELLPVFEFNELEYYSQIPGSDQYRFNF
WGYSTVNYFSPMGRFSAAVGQGAPARASCDEFKQLVKECHRRGIEVILDV
VFNHTAEGNERGPTISFRGLDNRVYYMLAPGGEYYNYSGCGNTLNCNQPV
VRQFILDCLKHWVTEYHVDGFRFDLASILTRAHSAWHPQQYDQETGQRVA
MSSGGAIVTAEGIMTDGAGVPTGYPLADPPLVESISEDPVLRNTKMIAEA
WDCDGLNQVGAFPHYGGRWSEWNGKFRDVVRNFIKGTDGPWAGDFASAIC
GSPNIYANNTPHETDWWANNGGRQWKGGRGPHASINFVAAHDGFTLADMV
AYNNKHNEANDGEQHNNSWNCGEEGPTTKWEVNRLRQRQMRNLTGALLLS
CGVPMINMGDEYGHSKNGNNNTYCHDSELNYLRWDQLAEDPHGFNRFVRL
LIHFRRATPALQRTTFVNDKDIQWHGELPNTPDWTDTSRLVAFTLHDGKG
GGLYVAFNTSHLPKLLQLPKWGGRVWQPLVDTSKVAPYDFLAVDGVLSAE
DVAAARRQMAMWTADHTYPVLPWSCIVLQSAPEDPAATSMIK
3D structure
PDB4okd Crystal Structure of the Chlamydomonas Starch Debranching Enzyme Isoamylase ISA1 Reveals Insights into the Mechanism of Branch Trimming and Complex Assembly.
ChainB
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) F77 R205 E308 F309 M340 D452 E527 D620
Catalytic site (residue number reindexed from 1) F1 R129 E230 F231 M262 D374 E449 D542
Enzyme Commision number 3.2.1.68: isoamylase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0019156 isoamylase activity
Biological Process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0009507 chloroplast

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4okd, PDBe:4okd, PDBj:4okd
PDBsum4okd
PubMed24993830
UniProtQ7X8Q2

[Back to BioLiP]