Structure of PDB 2w5v Chain A

Receptor sequence
>2w5vA (length=346) Species: 82349 (Antarctic bacterium TAB5) [Search protein sequence]
QLKTPKNVILLISDGAGLSQISSTFYFKSGTPNYTQFKNIGLIKTSSSRE
DVTDSASGATAFSCGIKTYNAAIGVADDSTAVKSIVEIAALNNIKTGVVA
TSSITDATPASFYAHALNRGLEEEIAMDMTESDLDFFAGGGLNYFTKRKD
KKDVLAILKGNQFTINTTALTDFSSIASNRKMGFLLADEAMPTMEKGRGN
FLSAATDLAIQFLSKDNSAFFIMSEGSQIDWGGHANNASYLISEINDFDD
AIGTALAFAKKDGNTLVIVTSDHETGGFTLAAKKNKREDGSEYSDYTEIG
PTFSTGGHSATLIPVFAYGPGSEEFIGIYENNEIFHKILKVTKWNQ
3D structure
PDB2w5v Coordination Sphere of the Third Metal Site is Essential to the Activity and Metal Selectivity of Alkaline Phosphatases.
ChainA
Resolution1.78 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D43 S84 D135 T137 R148 E254 D259 W260 H263 D301 H302 H337
Catalytic site (residue number reindexed from 1) D14 S55 D106 T108 R119 E225 D230 W231 H234 D272 H273 H308
Enzyme Commision number 3.1.3.1: alkaline phosphatase.
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 ZN A S84 D259 H263 H337 S55 D230 H234 H308
BS02 ZN A D43 S84 D301 H302 D14 S55 D272 H273
BS03 MG A D43 T137 E254 D14 T108 E225
BS04 MG A N266 S268 N237 S239
Gene Ontology
Molecular Function
GO:0004035 alkaline phosphatase activity
GO:0016791 phosphatase activity
GO:0046872 metal ion binding
Biological Process
GO:0016311 dephosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:2w5v, PDBe:2w5v, PDBj:2w5v
PDBsum2w5v
PubMed19916164
UniProtQ9KWY4

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