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Crystal structure of SLM1-pH domain in complex with phosphoserine

Analyse Crystal structure of SLM1-pH domain in complex with phosphoserine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4A6F
Type: protein
Length: 215 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphatidylinositol 4,5-bisphosphate-binding protein SLM1
UniProt: P40485
Ligands: SEP, PO4

Structure

x-ray diffraction · 2 distinct chains · 16% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphatidylinositol 4,5-bisphosphate-binding protein SLM1	protein	105	15% helix, 42% strand	P40485
B	Phosphatidylinositol 4,5-bisphosphate-binding protein SLM1	protein	110	16% helix, 39% strand	P40485

Ligands and binding sites

SEP · Phosphoserine · ligand · 4 copies · chains A, B
PO4 · Phosphate ion · ion · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

A–B · 325 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

4A6F · Crystal structure of Slm1-PH domain in complex with Phosphoserine · the same entry in another collection · chain A against A, TM-score 1.00
P40485 · AlphaFold monomer V2.0 prediction for phosphatidylinositol 4,5-bisphosphate-binding… · a predicted model of the same protein · chain A against A, TM-score 0.94

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 P40485
Elsewhere: RCSB PDB 4A6F · PDBe 4A6F · UniProt P40485

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