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Structure of a triple-helix region of human collagen type III from Trautec

Analyse Structure of a triple-helix region of human collagen type III from Trautec in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7XAN
Type: protein
Length: 78 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.5
Molecule: Collagen alpha-1(III) chain
UniProt: P02461

Structure

x-ray diffraction · resolution 1.5 · 3 distinct chains · 0% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Collagen alpha-1(III) chain	protein	26	0% helix, 0% strand	P02461
B	Collagen alpha-1(III) chain	protein	27	0% helix, 0% strand	P02461
C	Collagen alpha-1(III) chain	protein	25	0% helix, 0% strand	P02461

Interfaces

3 interfaces between chains.

A–B · 845 Å² buried · 10 hydrogen bonds · protein-protein
B–C · 825 Å² buried · 9 hydrogen bonds · protein-protein
A–C · 798 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 17 modified (hydroxylation).

Compared structures

7XAN · Structure of a triple-helix region of human collagen type III · the same entry in another collection · chain A against A, TM-score 1.00
P02461 · AlphaFold monomer V2.0 prediction for collagen alpha-1(III) chain (P02461) · a predicted model of the same protein · chain B against A, TM-score 0.41

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 P02461
Elsewhere: RCSB PDB 7XAN · PDBe 7XAN · UniProt P02461

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