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Solution structure of the coiled-coil trimerization domain from lung surfactant protein D

Analyse Solution structure of the coiled-coil trimerization domain from lung surfactant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1M7L
Type: protein
Length: 120 residues
Chains: 3
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pulmonary surfactant-associated protein D
UniProt: P35247
Pockets: 1 · best druggability 0.67

Structure

solution nmr · 1 distinct chain · 73% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Pulmonary surfactant-associated protein D	protein	40	73% helix, 0% strand	P35247

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	63	0.67	0.94	16	empty

Interfaces

3 interfaces between chains.

A–B · 676 Å² buried · 9 hydrogen bonds · protein-protein
A–C · 673 Å² buried · 8 hydrogen bonds · protein-protein
B–C · 666 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

1M7L · Solution Structure of the Coiled-Coil Trimerization Domain from Lung Surfactant Protein D · the same entry in another collection · chain A against A, TM-score 1.00
P35247 · AlphaFold monomer V2.0 prediction for pulmonary surfactant-associated protein D (P35247) · a predicted model of the same protein · chain A against A, TM-score 0.66

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 P35247
Elsewhere: RCSB PDB 1M7L · PDBe 1M7L · UniProt P35247

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