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Structure of the human collagen X NC1 trimer

Analyse Structure of the human collagen X NC1 trimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1GR3
Type: protein
Length: 132 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Collagen X
UniProt: Q03692
Ligands: CPS, CA, NA

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 58% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Collagen X	protein	132	0% helix, 58% strand	Q03692

Ligands and binding sites

CPS · 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate · ligand · chains A
CA · Calcium ion · metal · 2 copies · chains A
NA · Sodium ion · metal · chains A

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

Compared structures

1GR3 · Structure of the human collagen X NC1 trimer · the same entry in another collection · chain A against A, TM-score 1.00
Q03692 · AlphaFold monomer V2.0 prediction for collagen alpha-1(X) chain (Q03692) · a predicted model of the same protein · 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
Every structure of UniProt Q03692
Elsewhere: RCSB PDB 1GR3 · PDBe 1GR3 · UniProt Q03692

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