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Structure of the antibacterial peptide ABC transporter mcjd in an apo inward occluded conformation

Analyse Structure of the antibacterial peptide ABC transporter mcjd in an apo inward… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5OFP
Type: protein
Length: 571 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Microcin-J25 export ATP-BINDING/PERMEASE protein mcjd
UniProt: Q9X2W0
Pockets: 7 · best druggability 0.71

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Microcin-J25 export ATP-BINDING/PERMEASE protein mcjd	protein	571	61% helix, 10% strand	Q9X2W0

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	51	0.71	0.98	17	empty
2	425	0.65	0.78	29	empty
3	244	0.51	0.75	27	empty
4	91	0.43	0.79	17	empty
5	55	0.43	0.83	19	empty

Compared structures

5OFP · Structure of the antibacterial peptide ABC transporter McjD in an apo inward occluded… · the same entry in another collection · chain A against A, TM-score 1.00
Q9X2W0 · AlphaFold monomer V2.0 prediction for microcin-J25 export ATP- BINDING/PERMEASE protein… · a predicted model of the same protein · chain A against A, TM-score 0.92

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 Q9X2W0
Elsewhere: RCSB PDB 5OFP · PDBe 5OFP · UniProt Q9X2W0

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