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Crystal structure of PA1607, a putative transcription factor

Analyse Crystal structure of PA1607, a putative transcription factor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2F2E
Type: protein
Length: 282 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: PA1607
UniProt: Q9I3B4
Ligands: GLC, SO4
Pockets: 3 · best druggability 0.45

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	PA1607	protein	142	39% helix, 15% strand	Q9I3B4
B	PA1607	protein	140	42% helix, 15% strand	Q9I3B4

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · chains B
SO4 · Sulfate ion · ion · 4 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	106	0.45	0.79	23	empty
2	99	0.42	0.78	22	empty
3	62	0.31	0.75	19	empty

Interfaces

1 interface between chains.

A–B · 3278 Å² buried · 32 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

2F2E · Crystal Structure of PA1607, a Putative Transcription Factor · 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 Q9I3B4
Elsewhere: RCSB PDB 2F2E · PDBe 2F2E · UniProt Q9I3B4

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