Structure of PDB 4cr6 Chain D

Receptor sequence
>4cr6D (length=255) Species: 240 (Flavobacterium sp. 141-8) [Search protein sequence]
GRLAGKAAIVTGAAGGIGRATVEAYLREGASVVAMDLAPRLAATRYEEPG
AIPIACDLRAAIDAAMADAVARLGGLDILVAGGALKGGTGNFLDLSDADW
DRYVDVNMTGTFLTCRAGARAMVAAGARSARIITIGSVNSFMAEPEAAAY
VAAKGGVAMLTRAMAVDLARHGILVNMIAPGPVDVTGNNTGYSEPRLAEQ
VLDEVALGRPGLPEEVATAAVFLAEDGSSFITGSTITIDGGLSAMIFGGM
REGRR
3D structure
PDB4cr6 Crystal Structures and Functional Studies Clarify Substrate Selectivity and Catalytic Residues for the Unique Orphan Enzyme N-Acetyl-D-Mannosamine Dehydrogenase.
ChainD
Resolution1.9 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) G16 S137 Y150 K154
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 MAN D M158 E220 L258 M261 M142 E204 L242 M245
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0050123 N-acylmannosamine 1-dehydrogenase activity

View graph for
Molecular Function
External links
PDB RCSB:4cr6, PDBe:4cr6, PDBj:4cr6
PDBsum4cr6
PubMed24969681
UniProtP22441|DHMA_FLAS1 N-acylmannosamine 1-dehydrogenase

[Back to BioLiP]