Structure of PDB 2ya0 Chain A

Receptor sequence
>2ya0A (length=714) Species: 170187 (Streptococcus pneumoniae TIGR4) [Search protein sequence]
SWRLKDETYSYDGKLGADLKEEGKQVDLTLWSPSADKVSVVVYDKNDPDK
VVGTVALEKGERGTWKQTLDSTNKLGITDFTGYYYQYQIERQGKTVLALD
PYAKSLAAWNSDDSKIDDAHKVAKAAFVDPAKLGPQDLTYGKIHNFKTRE
DAVIYEAHVRDFTSDPAIAKDLTKPFGTFEAFIEKLDYLKDLGVTHIQLL
PVLSYYFVNELKNHERLSDYASSNSNYNWGYDPQNYFSLTGMYSSDPKNP
EKRIAEFKNLINEIHKRGMGAILDVVYNHTAKVDLFEDLEPNYYHFMDAD
GTPRTSFGGGRLGTTHHMTKRLLIDSIKYLVDTYKVDGFRFDMMGDHDAA
SIEEAYKAARALNPNLIMLGEGWRTYAGDENMPTKAADQDWMKHTDTVAV
FSDDIRNNLKSGYPNEGQPAFITGGKRDVNTIFKNLIAQPTNFEADSPGD
VIQYIAAHDNLTLFDIIAQSIKKDPSKAENYAEIHRRLRLGNLMVLTAQG
TPFIHSGQEYGRTKQFRNPAYRTPVAEDKVPNKSHLLRDKDGNPFDYPYF
IHDSYDSSDAVNKFDWTKATDGKAYPENVKSRDYMKGLIALRQSTDAFRL
KSLQDIKDRVHLITVPGQNGVEKEDVVIGYQITAPNGDIYAVFVNADEKA
REFNLGTAFAHLRNAEVLADENQAGPVGIANPKGLEWTEKGLKLNALTAT
VLRVSQNGTSHEST
3D structure
PDB2ya0 The Conformation and Function of a Multimodular Glycogen-Degrading Pneumococcal Virulence Factor.
ChainA
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) W90 S185 Y186 T221 D323 E352 D440
Catalytic site (residue number reindexed from 1) W109 S204 Y205 T240 D342 E371 D459
Enzyme Commision number 3.2.1.41: pullulanase.
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 CA A S206 Y208 D537 S225 Y227 D556
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2ya0, PDBe:2ya0, PDBj:2ya0
PDBsum2ya0
PubMed21565699
UniProtA0A0H2UNG0|PULA_STRPN Pullulanase A (Gene Name=spuA)

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