Structure of PDB 2ntq Chain A

Receptor sequence
>2ntqA (length=342) Species: 198628 (Dickeya dadantii 3937) [Search protein sequence]
ATTYNAVVSKSSSDGKTFKTIADAIASAPAGSTPFVILIKNGVYNERLTI
TRNNLHLKGESRNGAVIAAATAAGTLKSDGSKWGTAGSSTITISAKDFSA
QSLTIRNDFDFPANQAKSDSDSSKIKDTQAVALYVTKSGDRAYFKDVSLV
GYQDTLYVSGGRSFFSDCRISGTVDFIFGDGTALFNNCDLVSRYRADVKS
GNVSGYLTAPSTNINQKYGLVITNSRVIRESDSVPAKSYGLGRPWHPTTT
FSDGRYADPNAIGQTVFLNTSMDNHIYGWDKMSGKDKNGNTIWFNPEDSR
FFEYKSYGAGATVSKDRRQLTDAQAAEYTQSKVLGDWTPTLP
3D structure
PDB2ntq Molecular basis of the activity of the phytopathogen pectin methylesterase.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q153 Q177 D178 D199 R267
Catalytic site (residue number reindexed from 1) Q129 Q153 D154 D175 R243
Enzyme Commision number 3.1.1.11: pectinesterase.
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 ADA A Q177 D178 D199 M306 Q153 D154 D175 M282
BS02 ADA A T109 W269 T272 T85 W245 T248
BS03 ADA A T109 A110 P271 T272 T85 A86 P247 T248
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0030599 pectinesterase activity
GO:0052689 carboxylic ester hydrolase activity
Biological Process
GO:0042545 cell wall modification
GO:0045490 pectin catabolic process
GO:0071555 cell wall organization
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0009279 cell outer membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2ntq, PDBe:2ntq, PDBj:2ntq
PDBsum2ntq
PubMed17717531
UniProtP0C1A9|PMEA_DICD3 Pectinesterase A (Gene Name=pemA)

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