Structure of PDB 1o12 Chain B

Receptor sequence
>1o12B (length=363) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MIVEKVLIVDPIDGEFTGDVEIEEGKIVKVEKRECIPRGVLMPGFVDPHI
HGVVGADTMNCDFSEMEEFLYSQGVTTFLATTVSTSLEKMKEILRKARDY
ILENPSTSLLGVHLEGPYISKEKKGAHSEKHIRPPSERELSEIDSPAKML
TFAPEIESSELLLRLVKRDIVLSAGHSIATFEEFMKFYKEGVKRITHFPN
GLKPLHHREIGITGAGLLLDDVKLELICDGVHLSREMVKLVYKVKKANGI
VLVTDSISAAGLKDGTTTLGDLVVKVKDGVPRLEDGTLAGSTLFFSQAVK
NFRKFTGCSITELAKVSSYNSCVELGLDDRGRIAEGTRADLVLLDEDLNV
VMTIKEGEVVFRS
3D structure
PDB1o12 Crystal structure of N-acetylglucosamine-6-phosphate deacetylase (TM0814) from Thermotoga maritima at 2.5 A resolution
ChainB
Resolution2.5 Å
3D
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
Enzyme Commision number 3.5.1.25: N-acetylglucosamine-6-phosphate deacetylase.
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 FE B E115 H176 H197 E115 H176 H197
Gene Ontology
Molecular Function
GO:0008448 N-acetylglucosamine-6-phosphate deacetylase activity
GO:0016787 hydrolase activity
GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
GO:0046872 metal ion binding
Biological Process
GO:0006040 amino sugar metabolic process
GO:0006044 N-acetylglucosamine metabolic process
GO:0006046 N-acetylglucosamine catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1o12, PDBe:1o12, PDBj:1o12
PDBsum1o12
PubMed
UniProtQ9WZS1

[Back to BioLiP]