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4D64

Structure of porin Omp-Pst1 from P. stuartii; the crystallographic symmetry generates a dimer of trimers.

Functional Information from GO Data
ChainGOidnamespacecontents
A0006811biological_processmonoatomic ion transport
A0009279cellular_componentcell outer membrane
A0015288molecular_functionporin activity
A0016020cellular_componentmembrane
A0034220biological_processmonoatomic ion transmembrane transport
A0046930cellular_componentpore complex
B0006811biological_processmonoatomic ion transport
B0009279cellular_componentcell outer membrane
B0015288molecular_functionporin activity
B0016020cellular_componentmembrane
B0034220biological_processmonoatomic ion transmembrane transport
B0046930cellular_componentpore complex
C0006811biological_processmonoatomic ion transport
C0009279cellular_componentcell outer membrane
C0015288molecular_functionporin activity
C0016020cellular_componentmembrane
C0034220biological_processmonoatomic ion transmembrane transport
C0046930cellular_componentpore complex
Functional Information from PROSITE/UniProt
site_idPS00576
Number of Residues17
DetailsGRAM_NEG_PORIN General diffusion Gram-negative porins signature. IsvGsyYyFnKnmSAVV
ChainResidueDetails
AILE304-VAL320

217705

PDB entries from 2024-03-27

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