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Crystal structure of fkrp in complex with ba ion, ba-sad data

Analyse Crystal structure of fkrp in complex with ba ion, ba-sad data in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6L7U
Type: protein
Length: 1,758 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fukutin-related protein
EC: 2.4.2.-
UniProt: Q9H9S5
Ligands: NAG, ZN, BA
Pockets: 20 · best druggability 0.81

Structure

x-ray diffraction · 4 distinct chains · 30% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fukutin-related protein (EC 2.4.2.-)	protein	442	31% helix, 27% strand	Q9H9S5
B	Fukutin-related protein (EC 2.4.2.-)	protein	444	29% helix, 25% strand	Q9H9S5
C	Fukutin-related protein (EC 2.4.2.-)	protein	441	30% helix, 27% strand	Q9H9S5
D	Fukutin-related protein (EC 2.4.2.-)	protein	431	30% helix, 27% strand	Q9H9S5

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A, C, B, D
ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
BA · Barium ion · metal · 4 copies · chains A, B, C, D

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

Pockets

20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	611	0.81	0.86	85	empty
2	749	0.74	0.79	46	empty
3	580	0.74	0.81	48	empty
4	73	0.72	0.97	26	empty
5	611	0.71	0.79	47	empty

Interfaces

6 interfaces between chains.

A–B · 1549 Å² buried · 23 hydrogen bonds · protein-protein
C–D · 1474 Å² buried · 20 hydrogen bonds · protein-protein
A–C · 846 Å² buried · 9 hydrogen bonds · protein-protein
B–D · 674 Å² buried · 7 hydrogen bonds · protein-protein
B–C · 95 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 glycan, 4 disulfide (N-glycosylation, disulfide).

Compared structures

6L7U · Crystal structure of FKRP in complex with Ba ion, Ba-SAD data · the same entry in another collection · chain D against D, TM-score 1.00
Q9H9S5 · AlphaFold monomer V2.0 prediction for fukutin-related protein (Q9H9S5) · a predicted model of the same protein · chain D against A, TM-score 0.99

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 Q9H9S5
Elsewhere: RCSB PDB 6L7U · PDBe 6L7U · UniProt Q9H9S5

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