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Crystal structures of homooligomers of collagen type IV. ALPHA5NC1

Analyse Crystal structures of homooligomers of collagen type IV. ALPHA5NC1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5NAZ
Type: protein
Length: 226 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Collagen alpha-5(IV) chain
UniProt: P29400
Ligands: CL
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Collagen alpha-5(IV) chain	protein	226	10% helix, 42% strand	P29400

Ligands and binding sites

CL · Chloride ion · ion · 2 copies · chains A
PG4 · Tetraethylene glycol · additive · 2 copies · chains A

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

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	78	0.31	0.73	15	empty

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

5NAZ · Crystal structures of homooligomers of collagen type IV. alpha5NC1 · the same entry in another collection · chain A against A, TM-score 1.00
P29400 · AlphaFold monomer V2.0 prediction for collagen alpha-5(IV) chain (P29400) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P29400
Elsewhere: RCSB PDB 5NAZ · PDBe 5NAZ · UniProt P29400

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