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SH3 domain from mouse cortactin (C 2 2 21 crystal form)

Analyse SH3 domain from mouse cortactin (C 2 2 21 crystal form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5NV1
Type: protein
Length: 60 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Src substrate cortactin
UniProt: Q60598
Ligands: MG

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Src substrate cortactin	protein	60	5% helix, 45% strand	Q60598

Ligands and binding sites

MG · Magnesium ion · metal · chains A
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A
GOL · Glycerol · additive · chains A

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

Compared structures

5NV1 · SH3 domain from Mouse cortactin (C 2 2 21 crystal form) · the same entry in another collection · chain A against A, TM-score 1.00
Q60598 · AlphaFold monomer V2.0 prediction for src substrate cortactin (Q60598) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q60598
Elsewhere: RCSB PDB 5NV1 · PDBe 5NV1 · UniProt Q60598

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