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MolNFT v1 · #118453 · protein

Structure of rck domain with cda

5F29 · NA+/H+ antiporter-like protein: “Structure of rck domain with cda”. X-ray diffraction, 1 ligand (2BA), 1 pocket (best druggability 0.54). MolNFT v1 #118453 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
5F29
Type
protein
Length
141 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
NA+/H+ antiporter-like protein
UniProt
A0A077VS08
Ligands
2BA
Pockets
1 · best druggability 0.54

Structure

x-ray diffraction · 2 distinct chains · 25% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANA+/H+ antiporter-like proteinprotein7024% helix, 33% strandA0A077VS08
BNA+/H+ antiporter-like proteinprotein7125% helix, 32% strandA0A077VS08

Ligands and binding sites

  • 2BA · (2r,3r,3as,5r,7ar,9r,10r,10as,12r,14ar)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-D:3', 2'-J][1,3,7,9,2,8 ]tetraoxadiphosphacyclododecine-3,5, 10,12-tetrol 5,12-dioxide · ligand · chains A, B

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12090.540.78192BA

Interfaces

1 interface between chains.

  • A–B · 573 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (engineered).

Compared structures

  • 5F29 · Structure of RCK domain with cda · the same entry in another collection · chain A against A, TM-score 1.00

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