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Integrin binding CBEGF22-TB4-CBEGF33 fragment of human fibrillin-1, holo form.

Analyse Integrin binding CBEGF22-TB4-CBEGF33 fragment of human fibrillin-1, holo form. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1UZJ
Type: protein
Length: 486 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fibrillin-1
UniProt: P35555
Ligands: CA
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Fibrillin-1	protein	162	13% helix, 33% strand	P35555

Ligands and binding sites

CA · Calcium ion · metal · 6 copies · chains A, B, C

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	770	0.69	0.76	72	empty

Interfaces

2 interfaces between chains.

A–B · 218 Å² buried · 1 hydrogen bond · protein-protein
B–C · 61 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 30 disulfide (disulfide).

Compared structures

1UZJ · Integrin binding cbEGF22-TB4-cbEGF33 fragment of human fibrillin-1, holo form. · the same entry in another collection · 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 P35555
Elsewhere: RCSB PDB 1UZJ · PDBe 1UZJ · UniProt P35555

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