3POQ: OmpF protein

Crystal structure of E.coli OmpF porin in lipidic cubic phase: space group H32, small unit cell. Determined by X-ray diffraction at 1.9 Å resolution. Released 7 Mar 2012.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Escherichia coli
Chains: 1
Atoms: 3,038
Mol. weight: 45.49 kDa
Ligands: OLC, SCN
Released: 7 Mar 2012

Explore 3POQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3POQ contains 5 α-helices and 23 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 5 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	1
β-strand	9-23	15	1
β-strand	31	1	2
β-strand	36-37	2	1
β-strand	40-52	13	1
β-strand	55-66	12	1
β-strand	80-90	11	1
β-strand	94-102	9	1
α-helix	106-109	4
β-strand	132-141	10	1
α-helix	143-146	4
β-strand	151-158	8	1
β-strand	161	1	3
α-helix	166-168	3
β-strand	170	1	3
β-strand	173-182	10	1
β-strand	185-195	11	1
α-helix	196-197	2
α-helix	198-201	4
β-strand	205	1	1
β-strand	210-220	11	1
β-strand	225-242	18	1
β-strand	247-263	17	1
β-strand	269-283	15	1
β-strand	287-302	16	1
β-strand	307-316	10	1
β-strand	329	1	2
β-strand	331-339	9	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
OmpF protein	A	protein	340	Escherichia coli	P02931 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3POQ_1 OmpF protein (chains A)
AEIYNKDGNKVDLYGKAVGLHYFSKGNGENSYGGNGDMTYARLGFKGETQINSDLTGYGQ
WEYNFQGNNSEGADAQTGNKTRLAFAGLKYADVGSFDYGRNYGVVYDALGYTDMLPEFGG
DTAYSDDFFVGRVGGVATYRNSNFFGLVDGLNFAVQYLGKNERDTARRSNGDGVGGSISY
EYEGFGIVGAYGAADRTNLQEAQPLGNGKKAEQWATGLKYDANNIYLAANYGETRNATPI
TNKFTNTSGFANKTQDVLLVAQYQFDFGLRPSIAYTKSKAKDVEGIGDVDLVNYFEVGAT
YYFNKNMSTYVDYIINQIDSDNKLGVGSDDTVAVGIVYQF

Ligands and cofactors

ID	Name	Formula	Copies
OLC	(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate	C21 H40 O4	23
SCN	Thiocyanate ion	C N S	3

Primary citation

Structure of Escherichia coli OmpF porin from lipidic mesophase. Efremov, R.G., Sazanov, L.A. J Struct Biol (2012) 178:311-318. DOI 10.1016/j.jsb.2012.03.005 · PubMed

Other PDB entries of the same protein (UniProt P02931 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2ZFG 1.59 Å, Structure of OMPF PORIN
4GCS 1.87 Å, Crystal Structure of E. coli OmpF porin in complex with Ertapenem
4LSF 1.9 Å, Ion selectivity of OmpF soaked in 0.1M KBr
6ZHV 1.95 Å, Crystal structure of OmpF porin soaked in ciprofloxacin metaloantibiotic
4GCP 1.98 Å, Crystal Structure of E. coli OmpF porin in complex with Ampicillin
3POX 2.0 Å, Crystal Structure of E.coli OmpF porin in lipidic cubic phase: space group P1
6ZHP 2.05 Å, Crystal structure of OmpF porin soaked in ciprofloxacin metaloantibiotic
4LSI 2.09 Å, Ion selectivity of OmpF porin soaked in 0.3M KBr
4LSE 2.1 Å, Ion selectivity of OmpF porin soaked in 0.2M NaBr
1HXX 2.2 Å, Ompf porin mutant Y106F
4GCQ 2.2 Å, Crystal Structure of E. coli OmpF porin in complex with Carbenicillin
4LSH 2.2 Å, Ion selectivity of OmpF porin soaked in 0.2M KBr

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