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Structural basis for the phosphoserine-proline recognition by group IV ww domains

Analyse Structural basis for the phosphoserine-proline recognition by group IV ww… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1F8A
Type: protein
Length: 162 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidyl-prolyl cis-trans isomerase nima-interacting 1; Y(SEP)PT(SEP)S peptide
EC: 5.2.1.8
UniProt: Q13526
Pockets: 1 · best druggability 0.49

Structure

x-ray diffraction · 2 distinct chains · 23% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Peptidyl-prolyl cis-trans isomerase nima-interacting 1 (EC 5.2.1.8)	protein	155	25% helix, 23% strand	Q13526
C	Y(SEP)PT(SEP)S peptide	protein	7	0% helix, 0% strand	—

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	122	0.49	0.80	26	empty

Interfaces

1 interface between chains.

B–C · 537 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (phosphorylation).

Compared structures

1F8A · Structural basis for the phosphoserine-proline recognition by group IV ww domains · the same entry in another collection · chain B against B, 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 Q13526
Elsewhere: RCSB PDB 1F8A · PDBe 1F8A · UniProt Q13526

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