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Structure of the sthk carboxy-terminal region in complex with camp

Analyse Structure of the sthk carboxy-terminal region in complex with camp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4D7T
Type: protein
Length: 370 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: STHK_CNBD_CAMP
UniProt: E0RR11
Ligands: CMP
Pockets: 7 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	STHK_CNBD_CAMP	protein	197	47% helix, 19% strand	E0RR11
B	STHK_CNBD_CAMP	protein	173	32% helix, 19% strand	E0RR11

Ligands and binding sites

CMP · Adenosine-3',5'-cyclic-monophosphate · ligand · 2 copies · chains A, B

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

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	92	0.70	0.93	20	CMP
2	91	0.67	0.91	19	CMP
3	186	0.64	0.83	22	empty
4	78	0.50	0.83	22	empty
5	178	0.48	0.77	27	empty

Compared structures

4D7T · Structure of the SthK Carboxy-Terminal Region in complex with cAMP · 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 E0RR11
Elsewhere: RCSB PDB 4D7T · PDBe 4D7T · UniProt E0RR11

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