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Structure of PDB 2aw3 Chain B

Receptor sequence
>2aw3B (length=796) Species: 562 (Escherichia coli) [Search protein sequence]
SQPIFNDKQFQEALSRQWQRYGLNSAAEMTPRQWWLAVSEALAEMLRAQP
FAKPVANQRHVNYISMEFLIGRLTGNNLLNLGWYQDVQDSLKAYDINLTD
LLEEEIDPALGNGGLGRLAACFLDSMATVGQSATGYGLNYQYGLFRQSFV
DGKQVEAPDDWHRSNYPWFRHNEALDVQVGIGGKVTKDGRWEPEFTITGQ
AWDLPVVGYRNGVAQPLRLWQATHAHPFDLTKFNDGDFLRAEQQGINAEK
LTKVLYPNDNAFEGKKLRLMQQYFQCACSVADILRRHHLAGRKLHELADY
EVIQLNDTHPTIAIPELLRVLIDEHQMSWDDAWAITSKTFAYTNHTLMPE
ALERWDVKLVKGLLPRHMQIINEINTRFKTLVEKTWPGDEKVWAKLAVVH
DKQVHMANLCVVGGFAVNGVAALHSDLVVKDLFPEYHQLWPNKFHNVTNG
ITPRRWIKQCNPALAALLDKSLQKEWANDLDQLINLEKFADDAKFRQQYR
EIKQANKVRLAEFVKVRTGIEINPQAIFDIQIKRLHEYKRQHLNLLHILA
LYKEIRENPQADRVPRVFLFGAKAAPGYYLAKNIIFAINKVADVINNDPL
VGDKLKVVFLPDYCVSAAEKLIPAADISEQISTAGKEASGTGNMKLALNG
ALTVGTLDGANVEIAEKVGEENIFIFGHTVEQVKAILAKGYDPVKWRKKD
KVLDAVLKELESGKYSDGDKHAFDQMLHSIGKQGGDPYLVMADFAAYVEA
QKQVDVLYRDQEAWTRAAILNTARCGMFSSDRSIRDYQARIWQAKR
3D structure
PDB2aw3 X-ray studies on ternary complexes of maltodextrin phosphorylase.
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H345 K533 R534 K539 T641 K645
Catalytic site (residue number reindexed from 1) H345 K533 R534 K539 T641 K645
Enzyme Commision number 2.4.1.1: glycogen phosphorylase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004645 1,4-alpha-oligoglucan phosphorylase activity
GO:0008184 glycogen phosphorylase activity
GO:0016757 glycosyltransferase activity
GO:0030170 pyridoxal phosphate binding
GO:0031220 maltodextrin phosphorylase activity
GO:0042803 protein homodimerization activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0005980 glycogen catabolic process
GO:0030980 alpha-glucan catabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:2aw3, PDBe:2aw3, PDBj:2aw3
PDBsum2aw3
PubMed18164678
UniProtP00490|PHSM_ECOLI Maltodextrin phosphorylase (Gene Name=malP)

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