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Low resolution, molecular envelope structure of type I collagen in situ determined by fiber diffraction. single type I collagen molecule, post rigid body refinement, 'relaxed'

Analyse Low resolution, molecular envelope structure of type I collagen in situ… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3HR2
Type
protein
Length
3,134 residues
Chains
3
Method
fiber diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Collagen alpha-1(I) chain; Collagen alpha-2(I) chain
UniProt
P02454, P02466

Structure

fiber diffraction · 2 distinct chains · 0% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CCollagen alpha-1(I) chainprotein10540% helix, 0% strandP02454
BCollagen alpha-2(I) chainprotein10260% helix, 0% strandP02466

Interfaces

3 interfaces between chains.

  • A–B · 15118 Ų buried · 0 hydrogen bonds · protein-protein
  • A–C · 15062 Ų buried · 0 hydrogen bonds · protein-protein
  • B–C · 15027 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 312 modified (hydroxylation).

Compared structures

  • 3HR2 · Low resolution, molecular envelope structure of type I collagen in situ determined by… · the same entry in another collection · chain A against A, TM-score 1.00
  • P02466 · AlphaFold monomer V2.0 prediction for collagen alpha-2(I) chain (P02466) · a predicted model of the same protein · chain B against A, TM-score 0.04
  • P02454 · AlphaFold monomer V2.0 prediction for collagen alpha-1(I) chain (P02454) · a predicted model of the same protein · chain A against A, TM-score 0.04

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