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Ccaat-binding complex from aspergillus nidulans

Analyse Ccaat-binding complex from aspergillus nidulans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4G91
Type: protein
Length: 236 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hapb protein; Transcription factor hapc (eurofung); Hape
UniProt: P87249, Q5B5Z6, Q5AYY8
Pockets: 2 · best druggability 0.39

Structure

x-ray diffraction · 3 distinct chains · 66% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hapb protein	protein	28	61% helix, 0% strand	P87249
B	Transcription factor hapc (eurofung)	protein	91	73% helix, 4% strand	Q5B5Z6
C	Hape	protein	117	62% helix, 3% strand	Q5AYY8

Pockets

2 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	97	0.39	0.76	17	empty
2	58	0.31	0.76	13	empty

Interfaces

3 interfaces between chains.

B–C · 2928 Å² buried · 27 hydrogen bonds · protein-protein
A–B · 581 Å² buried · 13 hydrogen bonds · protein-protein
A–C · 381 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

4G91 · CCAAT-binding complex from Aspergillus nidulans · 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 P87249
Every structure of UniProt Q5B5Z6
Every structure of UniProt Q5AYY8
Elsewhere: RCSB PDB 4G91 · PDBe 4G91 · UniProt P87249 · UniProt Q5B5Z6 · UniProt Q5AYY8

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