Structure of PDB 6pid Chain A

Receptor sequence
>6pidA (length=346) Species: 1658765 (Marinobacter subterrani) [Search protein sequence]
LGSMKTVFSPLHSRRHVKTELDGGLLIEPHEKPSRAETILARVKDQALGE
ILEPEEFGLGPVKRVHTADYVSFLETCWDEWVAAGKRGEAIPTFWVGRGM
RARLPKDIDGRLGYYSLGADTSISDGTWEAARASANVALTAQKLVAEGER
AAFALCRPPGHHAHADVFGGYCFFNNAAIAAQAFRDQGYGKVAVLDVDFH
HGNGTQAIFYDRSDVLTISLHGDPDLVFPHFLGFEDETGEGDGEAYNLNI
VFPPDTPFSIWSQGLEKACERIRTFAPDALVVALGVDTFEEDPISFFKLT
SGDYLKLGKRLEQLGLPTVFTMEGGYDVDAIGVNAVNVMQGFEGKS
3D structure
PDB6pid Structure and Function of the Acetylpolyamine Amidohydrolase from the Deep Earth HalophileMarinobacter subterrani.
ChainA
Resolution1.546 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 ?
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 ZN A D195 H197 D284 D198 H200 D287
BS02 MG A E288 D324 D326 E291 D327 D329
BS03 MG A D104 D106 D107 D109
BS04 OKS A E17 D19 D117 H158 H159 Y168 D195 H197 Y323 E20 D22 D120 H161 H162 Y171 D198 H200 Y326 MOAD: ic50=380uM
PDBbind-CN: -logKd/Ki=4.54,Kd=29.0uM
Gene Ontology
Molecular Function
GO:0004407 histone deacetylase activity
GO:0046872 metal ion binding
Biological Process
GO:0006338 chromatin remodeling

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6pid, PDBe:6pid, PDBj:6pid
PDBsum6pid
PubMed31436969
UniProtA0A0J7JFD7

[Back to BioLiP]