Structure of PDB 1o8l Chain A

Receptor sequence
>1o8lA (length=352) Species: 556 (Dickeya chrysanthemi) [Search protein sequence]
ATDTGGYAATAGGNVTGAVSKTATSMQDIVNIIDAARLDANGKKVKGGAY
PLVITYTGNEDSLINAAAANICGQWSKDPRGVEIKEFTKGITIIGANGSS
ANFGIWIKKSSDVVVQNMRIGYLPGGAKDGDMIRVDDSPNVWVDHNELFA
ANHECDGTPDNDTTFESAVDIKGASNTVTVSYNYIHGVKKVGLDGSSSSD
TGRNITYHHNYYNDVNARLPLQRGGLVHAYNNLYTNITGSGLNVRQNGQA
LIENNWFEKAINPVTSRYDGKNFGTWVLKGNNITKPADFSTYSITWTADT
KPYVNADSWTSTGTFPTVAYNYSPVSAQCVKDKLPGYAGVGKNLATLTST
AC
3D structure
PDB1o8l Characterization and Implications of Ca2+ Binding to Pectate Lyase C
ChainA
Resolution2.2 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) D129 D131 A151 E166 D170 A217 R218 P220
Catalytic site (residue number reindexed from 1) D129 D131 A151 E166 D170 A217 R218 P220
Enzyme Commision number 4.2.2.2: pectate lyase.
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 CA A D131 E166 D170 C352 D131 E166 D170 C352
Gene Ontology
Molecular Function
GO:0016829 lyase activity
GO:0030570 pectate lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0045490 pectin catabolic process
Cellular Component
GO:0005576 extracellular region

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1o8l, PDBe:1o8l, PDBj:1o8l
PDBsum1o8l
PubMed12540845
UniProtP11073|PLYC_DICCH Pectate lyase C (Gene Name=pelC)

[Back to BioLiP]