Structure of PDB 1say Chain A

Receptor sequence
>1sayA (length=361) Species: 32060 (Phormidium lapideum) [Search protein sequence]
MEIGVPKEIKNQEFRVGLSPSSVRTLVEAGHTVFIETQAGIGAGFADQDY
VQAGAQVVPSAKDAWSREMVVKVKEPLPAEYDLMQKDQLLFTYLHLAAAR
ELTEQLMRVGLTAIAYETVELPNRSLPLLTPMSIIAGRLSVQFGARFLER
QQGGRGVLLGGVPGVKPGKVVILGGGVVGTEAAKMAVGLGAQVQIFDINV
ERLSYLETLFGSRVELLYSNSAEIETAVAEADLLIGAVLVPGRRAPILVP
ASLVEQMRTGSVIVDVAVDQGGCVETLHPTSHTQPTYEVFGVVHYGVPNM
PGAVPWTATQALNNSTLPYVVKLANQGLKALETDDALAKGLNVQAHRLVH
PAVQQVFPDLA
3D structure
PDB1say Analysis of the structure and substrate binding of Phormidium lapideum alanine dehydrogenase.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R15 K74 Y93 H95 E117 L121 P127 T130 D269
Catalytic site (residue number reindexed from 1) R15 K74 Y93 H95 E117 L121 P127 T130 D269
Enzyme Commision number 1.4.1.1: alanine dehydrogenase.
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 PYR A R15 K74 Y93 H95 R15 K74 Y93 H95
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0000286 alanine dehydrogenase activity
GO:0016491 oxidoreductase activity
Biological Process
GO:0006524 alanine catabolic process
GO:0042853 L-alanine catabolic process
Cellular Component
GO:0005886 plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1say, PDBe:1say, PDBj:1say
PDBsum1say
PubMed9665169
UniProtO52942

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