Structure of PDB 2j1n Chain A

Receptor sequence
>2j1nA (length=346) Species: 562 (Escherichia coli) [Search protein sequence]
AEVYNKDGNKLDLYGKVDGLHYFSDNKDVDGDQTYMRLGFKGETQVTDQL
TGYGQWEYQIQGNSAENENNSWTRVAFAGLKFQDVGSFDYGRNYGVVYDV
TSWTDVLPEFGGDTYGSDNFMQQRGNGFATYRNTDFFGLVDGLNFAVQYQ
GKNGNPSGEGFTSGVTNNGRDALRQNGDGVGGSITYDYEGFGIGGAISSS
KRTDAQNTAAYIGNGDRAETYTGGLKYDANNIYLAAQYTQTYNATRVGSL
GWANKAQNFEAVAQYQFDFGLRPSLAYLQSKGKNLGRGYDDEDILKYVDV
GATYYFNKNMSTYVDYKINLLDDNQFTRDAGINTDNIVALGLVYQF
3D structure
PDB2j1n Crystal Structure of Osmoporin Ompc from E. Coli at 2.0 A.
ChainA
Resolution2.0 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 MG A N319 L321 T334 N319 L321 T334
Gene Ontology
Molecular Function
GO:0001618 virus receptor activity
GO:0005515 protein binding
GO:0015288 porin activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0006811 monoatomic ion transport
GO:0006974 DNA damage response
GO:0034220 monoatomic ion transmembrane transport
GO:0046718 symbiont entry into host cell
GO:0046813 receptor-mediated virion attachment to host cell
GO:0120010 intermembrane phospholipid transfer
Cellular Component
GO:0009279 cell outer membrane
GO:0016020 membrane
GO:0046930 pore complex

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:2j1n, PDBe:2j1n, PDBj:2j1n
PDBsum2j1n
PubMed16949612
UniProtP06996|OMPC_ECOLI Outer membrane porin C (Gene Name=ompC)

[Back to BioLiP]