Structure of PDB 1e4o Chain B

Receptor sequence

>1e4oB (length=796) Species: 562 (Escherichia coli)

SQPIFNDKQFQEALSRQWQRYGLNSAAEMTPRQWWLAVSEALAEMLRAQP
FAKPVANQRHVNYISMEFLIGRLTGNNLLNLGWYQDVQDSLKAYDINLTD
LLEEEIDPALGNGGLGRLAACFLDSMATVGQSATGYGLNYQYGLFRQSFV
DGKQVEAPDDWHRSNYPWFRHNEALDVQVGIGGKVTKDGRWEPEFTITGQ
AWDLPVVGYRNGVAQPLRLWQATHAHPFDLTKFNDGDFLRAEQQGINAEK
LTKVLYPNDNHTAGKKLRLMQQYFQCACSVADILRRHHLAGRKLHELADY
EVIQLNDTHPTIAIPELLRVLIDEHQMSWDDAWAITSKTFAYTNHTLMPE
ALERWDVKLVKGLLPRHMQIINEINTRFKTLVEKTWPGDEKVWAKLAVVH
DKQVHMANLCVVGGFAVNGVAALHSDLVVKDLFPEYHQLWPNKFHNVTNG
ITPRRWIKQCNPALAALLDKSLQKEWANDLDQLINLEKFADDAKFRDQYR
EIKQANKVRLAEFVKVRTGIEINPQAIFDIQIKRLHEYKRQHLNLLHILA
LYKEIRENPQADRVPRVFLFGAKAAPGYYLAKNIIFAINKVADVINNDPL
VGDKLKVVFLPDYCVSAAEKLIPAADISEQISTAGKEASGTGNMKLALNG
ALTVGTLDGANVEIAEKVGEENIFIFGHTVEQVKAILAKGYDPVKWRKKD
KVLDAVLKELESGKYSDGDKHAFDQMLHSIGKQGGDPYLVMADFAAYVEA
QKQVDVLYRDQEAWTRAAILNTARCGMFSSDRSIRDYQARIWQAKR

3D structure

• PDB: 1e4o Phosphorylase Recognition and Phosphorylysis of its Oligosaccharide Substrate: Answers to a Long Outstanding Question
• Chain: B
• Resolution: 2.9 Å

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	BGC	B	E350 H536 Y578	E350 H536 Y578
BS02	GLC	B	E350 A575 Y578	E350 A575 Y578
BS03	GLC	B	N112 Y256 R268 H309 E350 R534	N112 Y256 R268 H309 E350 R534
BS04	GLC	B	E67 G113 G114 L115 D307 H345 T346 R534	E67 G113 G114 L115 D307 H345 T346 R534
BS05	GLC	B	L115 H345 N449 E637 G640	L115 H345 N449 E637 G640
BS06	PLP	B	R117 W456 K533 C614 V615 G640 T641 G642 K645	R117 W456 K533 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

External links

• PDB: RCSB:1e4o, PDBe:1e4o, PDBj:1e4o
• PDBsum: 1e4o
• PubMed: 10469642
• UniProt: P00490|PHSM_ECOLI Maltodextrin phosphorylase (Gene Name=malP)