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Crystal structure of a CMABCB1 mutant

Analyse Crystal structure of a CMABCB1 mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7DQV
Type: protein
Length: 589 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Probable ATP-dependent transporter YCF16
UniProt: M1VAN7
Ligands: ANP, MG, NO3
Pockets: 6 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 61% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Probable ATP-dependent transporter YCF16	protein	589	61% helix, 10% strand	M1VAN7

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
MG · Magnesium ion · metal · chains A
NO3 · Nitrate ion · ion · chains A
DMU · Decyl-beta-D-maltopyranoside · additive · 2 copies · chains A

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

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	488	0.67	0.78	41	empty
2	201	0.57	0.80	27	empty
3	64	0.49	0.85	14	empty
4	207	0.48	0.74	17	empty
5	106	0.45	0.78	19	empty

Compared structures

7DQV · Crystal structure of a CmABCB1 mutant · 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 M1VAN7
Elsewhere: RCSB PDB 7DQV · PDBe 7DQV · UniProt M1VAN7

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