1HXX: Ompf porin mutant Y106F

Ompf porin mutant Y106F. Determined by X-ray diffraction at 2.2 Å resolution. Released 6 Jun 2001.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Escherichia coli
Chains: 1
Atoms: 2,792
Mol. weight: 38.32 kDa
Ligands: C8E
Released: 6 Jun 2001

Explore 1HXX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1HXX contains 3 α-helices and 25 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: 3 helices, 25 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	40-50	11	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
β-strand	170	1	3
β-strand	173-182	10	1
β-strand	185-195	11	1
α-helix	198-201	4
β-strand	205	1	4
β-strand	210-222	13	1
β-strand	225-235	11	1
β-strand	239-242	4	4
β-strand	247-250	4	4
β-strand	253-263	11	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
Outer membrane protein F	A	protein	340	Escherichia coli	P02931 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1HXX_1 OUTER MEMBRANE PROTEIN F (chains A)
AEIYNKDGNKVDLYGKAVGLHYFSKGNGENSYGGNGDMTYARLGFKGETQINSDLTGYGQ
WEYNFQGNNSEGADAQTGNKTRLAFAGLKYADVGSFDYGRNYGVVFDALGYTDMLPEFGG
DTAYSDDFFVGRVGGVATYRNSNFFGLVDGLNFAVQYLGKNERDTARRSNGDGVGGSISY
EYEGFGIVGAYGAADRTNLQEAQPLGNGKKAEQWATGLKYDANNIYLAANYGETRNATPI
TNKFTNTSGFANKTQDVLLVAQYQFDFGLRPSIAYTKSKAKDVEGIGDVDLVNYFEVGAT
YYFNKNMSTYVDYIINQIDSDNKLGVGSDDTVAVGIVYQF

Ligands and cofactors

ID	Name	Formula	Copies
C8E	(hydroxyethyloxy)tri(ethyloxy)octane	C16 H34 O5	4

Primary citation

Role of charged residues at the OmpF porin channel constriction probed by mutagenesis and simulation. Phale, P.S., Philippsen, A., Widmer, C. et al. Biochemistry (2001) 40:6319-6325. DOI 10.1021/bi010046k · 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
3POQ 1.9 Å, Crystal structure of E.coli OmpF porin in lipidic cubic phase: space group H32, small…
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
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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