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The solution structure of the AMP-pnp bound nucleotide binding domain of kdpb

Analyse The solution structure of the AMP-pnp bound nucleotide binding domain of kdpb in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2A29
Type: protein
Length: 136 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Potassium-transporting ATPase B chain
EC: 3.6.3.12
UniProt: P03960
Ligands: ANP
Pockets: 1 · best druggability 0.40

Structure

solution nmr · 1 distinct chain · 37% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Potassium-transporting ATPase B chain (EC 3.6.3.12)	protein	136	37% helix, 32% strand	P03960

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 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	52	0.40	0.82	21	ANP

Compared structures

2A29 · The solution structure of the AMP-PNP bound nucleotide binding domain of KdpB · the same entry in another collection · chain A against A, TM-score 1.00
P03960 · AlphaFold monomer V2.0 prediction for potassium-transporting ATPase ATP-binding subunit… · a predicted model of the same protein · chain A against A, TM-score 0.93

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 P03960
Elsewhere: RCSB PDB 2A29 · PDBe 2A29 · UniProt P03960

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