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NMR structure of the ntr domain from human PCOLCE1

Analyse NMR structure of the ntr domain from human PCOLCE1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1UAP
Type: protein
Length: 131 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Procollagen C-proteinase enhancer protein
UniProt: Q15113
Pockets: 1 · best druggability 0.32

Structure

solution nmr · 1 distinct chain · 15% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Procollagen C-proteinase enhancer protein	protein	131	15% helix, 33% strand	Q15113

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	71	0.32	0.75	24	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

1UAP · NMR structure of the NTR domain from human PCOLCE1 · the same entry in another collection · chain A against A, TM-score 1.00
Q15113 · AlphaFold monomer V2.0 prediction for procollagen C-endopeptidase enhancer 1 (Q15113) · a predicted model of the same protein · chain A against A, TM-score 0.86

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 Q15113
Elsewhere: RCSB PDB 1UAP · PDBe 1UAP · UniProt Q15113

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