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Crystal structure of the apbe protein (TM1553) from thermotoga maritima MSB8 at 1.58 a resolution

Analyse Crystal structure of the apbe protein (TM1553) from thermotoga maritima MSB8 at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1VRM
Type: protein
Length: 309 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein TM1553
Ligands: UNL
Pockets: 2 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical protein TM1553	protein	309	36% helix, 28% strand	—

Ligands and binding sites

UNL · Unknown ligand · ligand · chains A
MPD · (4S)-2-methyl-2,4-pentanediol · additive · 2 copies · chains A
MRD · (4R)-2-methylpentane-2,4-diol · additive · chains A

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

Pockets

2 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	424	0.71	0.82	40	UNL
2	101	0.42	0.77	23	MPD

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

1VRM · Crystal structure of the apbe protein (tm1553) from thermotoga maritima msb8 at 1.58 A… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 1VRM · PDBe 1VRM

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