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Solution structure of an ABC collagen heterotrimer reveals a single- register helix stabilized by electrostatic interactions

Analyse Solution structure of an ABC collagen heterotrimer reveals a single- register… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2KLW
Type: protein
Length: 90 residues
Chains: 3
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: (PKG)10; (DOG)10; (POG)10
Ligands: ACE, NH2

Structure

solution nmr · 3 distinct chains · 0% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	(PKG)10	protein	30	0% helix, 0% strand	—
B	(DOG)10	protein	30	0% helix, 0% strand	—
C	(POG)10	protein	30	0% helix, 0% strand	—

Ligands and binding sites

ACE · Acetyl group · ligand · 3 copies · chains A, B, C
NH2 · Amino group · ion · 3 copies · chains A, B, C

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

Interfaces

3 interfaces between chains.

A–B · 1153 Å² buried · 23 hydrogen bonds · protein-protein
B–C · 891 Å² buried · 10 hydrogen bonds · protein-protein
A–C · 817 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 20 modified, 3 covalent (hydroxylation, covalent ligand).

Compared structures

2KLW · Solution structure of an abc collagen heterotrimer reveals a single-register helix… · the same entry in another collection · chain A against A, 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
Elsewhere: RCSB PDB 2KLW · PDBe 2KLW

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