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The structure of fis mutant PRO61ALA illustrates that the kink within the long alpha-helix is not due to the presence of the proline residue

Analyse The structure of fis mutant PRO61ALA illustrates that the kink within the long… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1FIP
Type: protein
Length: 154 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Factor for inversion stimulation (fis); Unknown peptide, possibly part of the unobserved…
UniProt: P11028

Structure

x-ray diffraction · 2 distinct chains · 66% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Factor for inversion stimulation (fis)	protein	73	70% helix, 0% strand	P11028
C, D	Unknown peptide, possibly part of the unobserved residues in entity 1	protein	4	0% helix, 0% strand	—

Interfaces

5 interfaces between chains.

A–B · 1666 Å² buried · 19 hydrogen bonds · protein-protein
B–C · 255 Å² buried · 0 hydrogen bonds · protein-protein
A–D · 246 Å² buried · 0 hydrogen bonds · protein-protein
B–D · 116 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 113 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

1FIP · The structure of fis mutant PRO61ALA illustrates that the kink within the long… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P11028
Elsewhere: RCSB PDB 1FIP · PDBe 1FIP · UniProt P11028

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