Research workbench

Refinement of BMP7 crystal structure

Analyse Refinement of BMP7 crystal structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LXI
Type: protein
Length: 104 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bone morphogenetic protein 7
UniProt: P18075
Ligands: NAG

Structure

x-ray diffraction · 1 distinct chain · 18% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bone morphogenetic protein 7	protein	104	18% helix, 45% strand	P18075

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A

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

Modifications

Observed in the structure: 3 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

1LXI · Refinement of BMP7 crystal structure · the same entry in another collection · chain A against A, TM-score 1.00
P18075 · AlphaFold monomer V2.0 prediction for bone morphogenetic protein 7 (P18075) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 P18075
Elsewhere: RCSB PDB 1LXI · PDBe 1LXI · UniProt P18075

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.