Structure of PDB 4cr8 Chain G

Receptor sequence
>4cr8G (length=262) Species: 240 (Flavobacterium sp. 141-8) [Search protein sequence]
PGRLAGKAAIVTGAAGGIGRATVEAYLREGASVVAMDLAPRLAATRYEEP
GAIPIACDLADRAAIDAAMADAVARLGGLDILVAGGALKGGTGNFLDLSD
ADWDRYVDVNMTGTFLTCRAGARAMVAAGAGKDGRSARIITIGSVNSFMA
EPEAAAYVAAKGGVAMLTRAMAVDLARHGILVNMIAPGPVDVTGNNTGYS
EPRLAEQVLDEVALGRPGLPEEVATAAVFLAEDGSSFITGSTITIDGGLS
AMIFGGMREGRR
3D structure
PDB4cr8 Crystal Structures and Functional Studies Clarify Substrate Selectivity and Catalytic Residues for the Unique Orphan Enzyme N-Acetyl-D-Mannosamine Dehydrogenase.
ChainG
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) G26 S153 Y166 K170
Catalytic site (residue number reindexed from 1) G17 S144 Y157 K161
Enzyme Commision number 1.1.1.233: N-acylmannosamine 1-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 NAD G G25 G26 I27 D46 L47 R50 D67 L68 G95 A96 G16 G17 I18 D37 L38 R41 D58 L59 G86 A87
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0050123 N-acylmannosamine 1-dehydrogenase activity

View graph for
Molecular Function
External links
PDB RCSB:4cr8, PDBe:4cr8, PDBj:4cr8
PDBsum4cr8
PubMed24969681
UniProtP22441|DHMA_FLAS1 N-acylmannosamine 1-dehydrogenase

[Back to BioLiP]