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Structure of signal transduction protein, NMR, minimized average structure

Analyse Structure of signal transduction protein, NMR, minimized average structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1NLP
Type: protein
Length: 62 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: C-src; NL2 (MN8-MN1-plpplp)
EC: 2.7.1.112
UniProt: P00525
Ligands: ACE, MN8, MN1, NH2

Structure

solution nmr · 2 distinct chains · 5% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C	C-src (EC 2.7.1.112)	protein	56	5% helix, 45% strand	P00525
N	NL2 (MN8-MN1-plpplp)	protein	6	0% helix, 0% strand	—

Ligands and binding sites

ACE · Acetyl group · ligand · chains C
MN8 · 2-(4-carcoxy-5-isopropylthiazolyl)benzopiperidine · ligand · chains C
MN1 · 4-carboxypiperidine · ligand · chains C, N
NH2 · Amino group · ion · chains C, N

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

Interfaces

1 interface between chains.

C–N · 316 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

1NLP · Structure of signal transduction protein, NMR, minimized average structure · the same entry in another collection · chain C against C, 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 P00525
Elsewhere: RCSB PDB 1NLP · PDBe 1NLP · UniProt P00525

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