Structure of PDB 2fni Chain A

Receptor sequence
>2fniA (length=374) Species: 85962 (Helicobacter pylori 26695) [Search protein sequence]
MKEFAYSEPCLDKEDKKAVLEVLNSKQLTQGKRSLLFEEALCEFLGVKHA
LVFNSATSALLTLYRNFSEFSADRNEIITTPISFVATANMLLESGYTPVF
AGIKNDGNIDELALEKLINERTKAIVSVDYAGKSVEVESVQKLCKKHSLS
FLSDSSHALGSEYQNKKVGGFALASVFSFHAIKPITTAEGGAVVTNDSEL
HEKMKLFRSHGMLKKDFFEGEVKSIGHNFRLNEIQSALGLSQLKKAPFLM
QKREEAALTYDRIFKDNPYFTPLHPLLKDKSSNHLYPILMHQKFFTCKKL
ILESLHKRGILAQVHYKPIYQYQLYQQLFNTAPLKSAEDFYHAEISLPCH
ANLNLESVQNIAHSVLKTFESFKI
3D structure
PDB2fni Structural and Functional Characterization of PseC, an Aminotransferase Involved in the Biosynthesis of Pseudaminic Acid, an Essential Flagellar Modification in Helicobacter pylori
ChainA
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F84 D154 H157 H180 K183 K214 G220 R230
Catalytic site (residue number reindexed from 1) F84 D154 H157 H180 K183 K214 G220 R230
Enzyme Commision number 2.6.1.92: UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase.
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 A A56 T57 F84 D154 S156 H157 S178 K183 A56 T57 F84 D154 S156 H157 S178 K183
Gene Ontology
Molecular Function
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:2fni, PDBe:2fni, PDBj:2fni
PDBsum2fni
PubMed16421095
UniProtO25130|PSEC_HELPY UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase (Gene Name=pseC)

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