Structure of PDB 2nst Chain A

Receptor sequence

>2nstA (length=342) Species: 198628 (Dickeya dadantii 3937)

ATTYNAVVSKSSSDGKTFKTIADAIASAPAGSTPFVILIKNGVYNERLTI
TRNNLHLKGESRNGAVIAAATAAGTLKSDGSKWGTAGSSTITISAKDFSA
QSLTIRNDFDFPANQAKSDSDSSKIKDTQAVALYVTKSGDRAYFKDVSLV
GYQATLYVSGGRSFFSDCRISGTVDFIFGDGTALFNNCDLVSRYRADVKS
GNVSGYLTAPSTNINQKYGLVITNSRVIRESDSVPAKSYGLGRPWHPTTT
FSDGRYADPNAIGQTVFLNTSMDNHIYGWDKMSGKDKNGNTIWFNPEDSR
FFEYKSYGAGATVSKDRRQLTDAQAAEYTQSKVLGDWTPTLP

3D structure

• PDB: 2nst Molecular basis of the activity of the phytopathogen pectin methylesterase.
• Chain: A
• Resolution: 1.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Q153 Q177 A178 D199 R267
• Catalytic site (residue number reindexed from 1): Q129 Q153 A154 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	M8C	A	R219 V227 S228 G229 Y230	R195 V203 S204 G205 Y206
BS02	M8C	A	Q177 V198 R267	Q153 V174 R243
BS03	M8C	A	Q153 Q177 D199 F202 M306	Q129 Q153 D175 F178 M282
BS04	ADA	A	T109 Q153 W269 P271 T272	T85 Q129 W245 P247 T248
BS05	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

External links

• PDB: RCSB:2nst, PDBe:2nst, PDBj:2nst
• PDBsum: 2nst
• PubMed: 17717531
• UniProt: P0C1A9|PMEA_DICD3 Pectinesterase A (Gene Name=pemA)