Structure of PDB 3gr9 Chain D

Receptor sequence
>3gr9D (length=381) Species: 562 (Escherichia coli) [Search protein sequence]
SSTWDDLEYKAIQSVLDSKMFTMGEYVKQYETQFAKTFGSKYAVMVSSGS
TANLLMIAALFFTKKPRLKKGDEIIVPAVSWSTTYYPLQQYGLRVKFVDI
DINTLNIDIESLKEAVTDSTKAILTVNLLGNPNNFDEINKIIGGRDIILL
EDNCESMGATFNNKCAGTFGLMGTFSSFYNKHIATMEGGCIVTDDEEIYH
ILLCIRAHGWTRNLPKKNKVTGVKSDDQFEESFKFVLPGYNVRPLEMSGA
IGIEQLKKLPRFISVRRKNAEYFLDKFKDHPYLDVQQETGESSWFGFSFI
IKKDSGVIRKQLVENLNSAGIECRPIVTGNFLKNTDVLKYFDYTVHNNVD
NAEYLDKNGLFVGNHQIELFDEIDYLREVLK
3D structure
PDB3gr9 Two Site-Directed Mutations Are Required for the Conversion of a Sugar Dehydratase into an Aminotransferase.
ChainD
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) W88 D159 E162 F185 K188 V230 F240 R250
Catalytic site (residue number reindexed from 1) W81 D152 E155 F178 K181 V223 F233 R243
Enzyme Commision number ?
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 AKG D H215 R250 H208 R243
BS02 AKG D W88 F185 X188 R331 W81 F178 X181 R324
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0000271 polysaccharide biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3gr9, PDBe:3gr9, PDBj:3gr9
PDBsum3gr9
PubMed19402712
UniProtB1B4V9

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