Structure of PDB 2iuc Chain B

Receptor sequence
>2iucB (length=342) Species: 82349 (Antarctic bacterium TAB5) [Search protein sequence]
QLKTPKNVILLISDGAGLSQISSTFYFKSGTPNYTQFKNIGLIKTSSSRE
DVTDSASGATAFSCGIKTYNAAIGVADDSTAVKSIVEIAALNSIKTGVVA
TSSITHATPASFYAHALNRGLEEEIAMDMTESDLDFFAGGGLNYFTSRSD
SKDVLAILKGNQFTINTTGLTDFSSIASNRKMGFLLADEAMPTMEKGRGN
FLSAATDLAIQFLSKDNSAFFIMSEGSQIDWGGHANNASYLISEINDFDD
AIGTALAFAKSDGNTLVIVTSDHETGGFTLAAKSNKSEYSDYTEIGPTFS
TGGHSATLIPVFAYGPGSEEFIGIYENNEIFHKILKVTKWNQ
3D structure
PDB2iuc Crystal Structure of Alkaline Phosphatase from the Antarctic Bacterium Tab5.
ChainB
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D43 S84 H135 T137 R148 E254 D259 W260 H263 D301 H302 H337
Catalytic site (residue number reindexed from 1) D14 S55 H106 T108 R119 E225 D230 W231 H234 D272 H273 H304
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 B D259 H263 H337 D230 H234 H304
BS02 ZN B D43 S84 D301 H302 D14 S55 D272 H273
BS03 MG B D43 T137 E254 D14 T108 E225
BS04 MG B H144 E153 D157 H115 E124 D128
BS05 MG B N266 S268 N237 S239
BS06 PO4 B S84 R148 H337 S55 R119 H304
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:2iuc, PDBe:2iuc, PDBj:2iuc
PDBsum2iuc
PubMed17198711
UniProtQ9KWY4

[Back to BioLiP]