Structure of PDB 3e2d Chain A

Receptor sequence
>3e2dA (length=502) Species: 169049 (Vibrio sp. G15-21) [Search protein sequence]
AEIKNVILMIGDGMGPQQVGLLETYANQAPNSIYKGNKTAIYQLAQEGVI
GSSLTHPEDAIVVDSACSATMLATGIYSSSEVIGIDSQGNHVETVLEKAK
KAGKATGLVSDTRLTHATPASFAAHQPHRSLENQIASDMLATGADVMLSG
GLRHWIPKSTNDKGETYKQLEKLTQGDVYLKSKRKDDRNLLTEAEKDGYQ
LAFNRNMLDDAKGDKLLGLFAYSGMDDGIAYSNKKKSGERTQPSLKEMTQ
KALNILSKDEDGFFLMVEGGQIDWAGHSNDAGTMLHELLKFDEAIQTVYE
WAKDREDTIVIVTADHETGSFGFSYSSNDLPKPQKRSGEAFADRDYAPNF
NFGAFDILDGLYNQKQSYYGMISEFQKLDKSLQTPEKLAEIVNKNSEFPI
TAEQAKNVLASKPNPYRLAQHKYLSAEEVPAINDFDAFFPYNDRGNLLAR
EQATGQNIVWGTGTHTHTPVNVFAWGPAEKILPVSKIMHHSELGEYIKQQ
VN
3D structure
PDB3e2d The 1.4 A crystal structure of the large and cold-active Vibrio sp. alkaline phosphatase.
ChainA
Resolution1.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D12 S65 H116 T118 R129 E268 D273 W274 H277 D315 H316 H465
Catalytic site (residue number reindexed from 1) D12 S65 H116 T118 R129 E268 D273 W274 H277 D315 H316 H465
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 D273 H277 H465 D273 H277 H465
BS02 ZN A D12 S65 D315 H316 D12 S65 D315 H316
BS03 MG A D12 T118 E268 D12 T118 E268
Gene Ontology
Molecular Function
GO:0004035 alkaline phosphatase activity
GO:0016791 phosphatase activity
GO:0046872 metal ion binding
Biological Process
GO:0016311 dephosphorylation

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:3e2d, PDBe:3e2d, PDBj:3e2d
PDBsum3e2d
PubMed18977465
UniProtQ93P54

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