Structure of PDB 1qm5 Chain A

Receptor sequence
>1qm5A (length=796) Species: 562 (Escherichia coli) [Search protein sequence]
SQPIFNDKQFQEALSRQWQRYGLNSAAEMTPRQWWLAVSEALAEMLRAQP
FAKPVANQRHVNYISMEFLIGRLTGNNLLNLGWYQDVQDSLKAYDINLTD
LLEEEIDPALGNGGLGRLAACFLDSMATVGQSATGYGLNYQYGLFRQSFV
DGKQVEAPDDWHRSNYPWFRHNEALDVQVGIGGKVTKDGRWEPEFTITGQ
AWDLPVVGYRNGVAQPLRLWQATHAHPFDLTKFNDGDFLRAEQQGINAEK
LTKVLYPNDNHTAGKKLRLMQQYFQCACSVADILRRHHLAGRKLHELADY
EVIQLNDTHPTIAIPELLRVLIDEHQMSWDDAWAITSKTFAYTNHTLMPE
ALERWDVKLVKGLLPRHMQIINEINTRFKTLVEKTWPGDEKVWAKLAVVH
DKQVHMANLCVVGGFAVNGVAALHSDLVVKDLFPEYHQLWPNKFHNVTNG
ITPRRWIKQCNPALAALLDKSLQKEWANDLDQLINLEKFADDAKFRDQYR
EIKQANKVRLAEFVKVRTGIEINPQAIFDIQIKRLHEYKRQHLNLLHILA
LYKEIRENPQADRVPRVFLFGAKAAPGYYLAKNIIFAINKVADVINNDPL
VGDKLKVVFLPDYCVSAAEKLIPAADISEQISTAGKEASGTGNMKLALNG
ALTVGTLDGANVEIAEKVGEENIFIFGHTVEQVKAILAKGYDPVKWRKKD
KVLDAVLKELESGKYSDGDKHAFDQMLHSIGKQGGDPYLVMADFAAYVEA
QKQVDVLYRDQEAWTRAAILNTARCGMFSSDRSIRDYQARIWQAKR
3D structure
PDB1qm5 Phosphorylase Recognition and Phosphorolysis of its Oligosaccharide Substrate: Answers to a Long Outstanding Question
ChainA
Resolution2.0 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
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 GLC A E350 H536 E350 H536 PDBbind-CN: -logKd/Ki=5.82,Ki=1.5uM
BS02 GLC A E350 R534 Y578 E350 R534 Y578 PDBbind-CN: -logKd/Ki=5.82,Ki=1.5uM
BS03 GLC A N112 Y256 R268 H309 R534 N112 Y256 R268 H309 R534 PDBbind-CN: -logKd/Ki=5.82,Ki=1.5uM
BS04 SGC A E67 G113 G114 L115 Y256 D307 T346 R534 E67 G113 G114 L115 Y256 D307 T346 R534 PDBbind-CN: -logKd/Ki=5.82,Ki=1.5uM
BS05 PO4 A G113 G114 R534 K539 G113 G114 R534 K539
BS06 GLC A G114 L115 H345 N449 E637 G640 G114 L115 H345 N449 E637 G640 PDBbind-CN: -logKd/Ki=5.82,Ki=1.5uM
BS07 PLP A L69 G113 G114 W456 K533 Y613 C614 V615 G640 T641 G642 K645 L69 G113 G114 W456 K533 Y613 C614 V615 G640 T641 G642 K645
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1qm5, PDBe:1qm5, PDBj:1qm5
PDBsum1qm5
PubMed10469642
UniProtP00490|PHSM_ECOLI Maltodextrin phosphorylase (Gene Name=malP)

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