Structure of PDB 3ss9 Chain X

Receptor sequence
>3ss9X (length=431) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
QYPLVKDLVALKETTWFNPGTTSLAEGLPYVGLTEQDVQDAHARLSRFAP
YLAKAFPETAATGGIIESELVAIPAMQKRLEKEYQQPISGQLLLKKDSHL
PISGSIKARGGIYEVLAHAEKLALEAGLLTLDDDYSKLLSPEFKQFFSQY
SIAVGSTGNLGLSIGIMSARIGFKVTVHMSADARAWKKAKLRSHGVTVVE
YEQDYGVAVEEGRKAAQSDPNCFFIDDENSRTLFLGYSVAGQRLKAQFAQ
QGRIVDADNPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPC
MLLGVHTGLHDQISVQDIGIDNLTAADGLAVGRASGFVGRAMERLLDGFY
TLSDQTMYDMLGWLAQEEGIRLEPSALAGMAGPQRVCASVSYQQMHGFSA
EQLRNTTHLVWATGGGMVPEEEMNQYLAKGR
3D structure
PDB3ss9 Crystal structure of D-serine dehydratase from Escherichia coli.
ChainX
Resolution1.97 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.3.1.18: D-serine ammonia-lyase.
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 PLP X I117 K118 N170 G279 V280 G281 G283 P284 L340 T424 I106 K107 N159 G268 V269 G270 G272 P273 L329 T413
Gene Ontology
Molecular Function
GO:0008721 D-serine ammonia-lyase activity
GO:0016829 lyase activity
GO:0016836 hydro-lyase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0006520 amino acid metabolic process
GO:0006974 DNA damage response
GO:0009097 isoleucine biosynthetic process
GO:0036088 D-serine catabolic process
GO:0046416 D-amino acid metabolic process
GO:0051410 detoxification of nitrogen compound
GO:0070178 D-serine metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:3ss9, PDBe:3ss9, PDBj:3ss9
PDBsum3ss9
PubMed22197591
UniProtP00926|SDHD_ECOLI D-serine dehydratase (Gene Name=dsdA)

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