Research workbench

SAP/SH2D1A bound to peptide N-py

Analyse SAP/SH2D1A bound to peptide N-py in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1KA6
Type: protein
Length: 115 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SH2 domain protein 1A; Peptide N-py
UniProt: O60880, Q13291
Ligands: NH2

Structure

solution nmr · 2 distinct chains · 16% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SH2 domain protein 1A	protein	107	17% helix, 25% strand	O60880
B	Peptide N-py	protein	8	0% helix, 13% strand	Q13291

Ligands and binding sites

NH2 · Amino group · ion · chains A, B

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

Interfaces

1 interface between chains.

A–B · 598 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

1KA6 · SAP/SH2D1A bound to peptide n-pY · the same entry in another collection · chain A against A, TM-score 1.00
O60880 · AlphaFold monomer V2.0 prediction for SH2 domain-containing protein 1A (O60880) · a predicted model of the same protein · chain A against A, TM-score 0.92
Q13291 · AlphaFold monomer V2.0 prediction for signaling lymphocytic activation molecule (Q13291) · a predicted model of the same protein · chain B against A, TM-score 0.44

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 O60880
Every structure of UniProt Q13291
Elsewhere: RCSB PDB 1KA6 · PDBe 1KA6 · UniProt O60880 · UniProt Q13291

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