Structure of PDB 5jlr Chain A

Receptor sequence
>5jlrA (length=396) Species: 243243 (Mycobacterium avium 104) [Search protein sequence]
PKVSVLITVTGVDQPGVTATLFEVLSRHGVELLNVEQVVIRHRLTLGVLV
CCPADVADGPALRHDVEAAIRKVGLDVSIERSDDVPIIREPSTHTIFVLG
RPITAAAFGAVAREVAALGVNIDLIRGVSDYPVIGLELRVSVPPGADGAL
RTALNRVSSEEHVDVAVEDYTLERRAKRLIVFDVDSTLVQGEVIEMLAAK
AGAEGQVAAITDAAMRGELDFAQSLQQRVATLAGLPATVIDEVAGQLELM
PGARTTLRTLRRLGYACGVVSGGFRRIIEPLAEELMLDYVAANELEIVDG
TLTGRVVGPIIDRAGKATALREFAQRAGVPMAQTVAVGDGANDIDMLAAA
GLGIAFNAKPALREVADASLSHPYLDTVLFLLGVTRGEIEAADAID
3D structure
PDB5jlr SAD phasing using iodide ions in a high-throughput structural genomics environment.
ChainA
Resolution2.261 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D187 V188 D189 G276 K320 D347
Catalytic site (residue number reindexed from 1) D183 V184 D185 G272 K316 D343
Enzyme Commision number 3.1.3.3: phosphoserine 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 MG A D187 D189 D343 D183 D185 D339
BS02 SER A D17 Q18 T22 D13 Q14 T18
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0016787 hydrolase activity
GO:0036424 L-phosphoserine phosphatase activity
GO:0046872 metal ion binding
Biological Process
GO:0006564 L-serine biosynthetic process
GO:0016311 dephosphorylation
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5jlr, PDBe:5jlr, PDBj:5jlr
PDBsum5jlr
PubMed
UniProtA0QJI1|SERB_MYCA1 Phosphoserine phosphatase (Gene Name=serB)

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