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Crystal structure of oligopeptide ABC transporter, periplasmic oligopeptide-binding protein (TM1226) from thermotoga maritima at 2.0 a resolution

Analyse Crystal structure of oligopeptide ABC transporter, periplasmic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5HM4
Type: protein
Length: 540 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mannoside ABC transport system, sugar-binding protein
UniProt: G4FEC0
Ligands: CA
Pockets: 4 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Mannoside ABC transport system, sugar-binding protein	protein	540	35% helix, 20% strand	G4FEC0

Ligands and binding sites

CA · Calcium ion · metal · chains B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1098	0.74	0.77	89	empty
2	148	0.43	0.75	23	empty
3	59	0.41	0.81	20	empty
4	60	0.40	0.80	15	empty

Compared structures

5HM4 · Crystal structure of oligopeptide ABC transporter, periplasmic oligopeptide-binding… · the same entry in another collection · chain B against B, 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 G4FEC0
Elsewhere: RCSB PDB 5HM4 · PDBe 5HM4 · UniProt G4FEC0

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