Structure of PDB 2ya2 Chain A

Receptor sequence
>2ya2A (length=708) Species: 170187 (Streptococcus pneumoniae TIGR4) [Search protein sequence]
TSWRLKDETYSYDGKLGADLKEEGKQVDLTLWSPSADKVSVVVYDKNDPD
KVVGTVALEKGERGTWKQTLDSTNKLGITDFTGYYYQYQIERQGKTVLAL
DPYAKSLAAWNSDDSKIDDAHKVAKAAFVDPAKLGPQDLTYGKIHNFKTR
EDAVIYEAHVRDFTSDPAIAKDLTKPFGTFEAFIEKLDYLKDLGVTHIQL
LPVLSYYFVNELKNHERLSDYASSNSNYNWGYDPQNYFSLTGMYSSDPKN
PEKRIAEFKNLINEIHKRGMGAILDVVYNHTAKVDLFEDLEPNYYHFMDA
DGTPRTSFGGGRLGTTHHMTKRLLIDSIKYLVDTYKVDGFRFDMMGDHDA
ASIEEAYKAARALNPNLIMLGEGWRTYAGDENMPTKAADQDWMKHTDTVA
VFSDDIRNNLKSGYPNEGQPAFITGGKRDVNTIFKNLIAQPTNFEADSPG
DVIQYIAAHDDLTLFDIIAQSIKKDPSKAENYAEIHRRLRLGNLMVLTAQ
GTPFIHSGQEYGRTKQFRNPAYRTPVAEDKVPNKSHLLRDKDGNPFDYPY
FIHDSYDSSDAVNKFDWTKATDGKAYPENVKSRDYMKGLIALRQSTDAFR
LKSLQDIKDRVHLITVPGQNGVEKEDVVIGYQITAPNGDIYAVFVNADEK
AREFNLGTAFAHLRNAEVLADENQAGPVGIANPKGLEWTEKGLKLNALTA
TVLRVSQN
3D structure
PDB2ya2 The Conformation and Function of a Multimodular Glycogen-Degrading Pneumococcal Virulence Factor.
ChainA
Resolution2.37 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) W110 S205 Y206 T241 D343 E372 D460
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 NOJ A W210 Y212 F288 D323 M324 E352 H439 D440 W230 Y232 F308 D343 M344 E372 H459 D460
BS02 GLC A Y212 D213 D534 Y536 Y232 D233 D554 Y556
BS03 CA A M373 T376 D377 D427 D431 M393 T396 D397 D447 D451
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:2ya2, PDBe:2ya2, PDBj:2ya2
PDBsum2ya2
PubMed21565699
UniProtA0A0H2UNG0|PULA_STRPN Pullulanase A (Gene Name=spuA)

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