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Prim-pol domain of CRISPR-associated prim-pol (capp) from marinitoga sp. 1137

Analyse Prim-pol domain of CRISPR-associated prim-pol (capp) from marinitoga sp. 1137 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7NQD
Type: protein
Length: 420 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: TPR_REGION domain-containing protein
UniProt: H2J4R1
Pockets: 4 · best druggability 0.44

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	TPR_REGION domain-containing protein	protein	207	35% helix, 27% strand	H2J4R1
B	TPR_REGION domain-containing protein	protein	213	34% helix, 28% strand	H2J4R1

Pockets

4 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	173	0.44	0.74	24	empty
2	105	0.42	0.77	16	empty
3	113	0.40	0.76	19	empty
4	53	0.25	0.73	10	empty

Interfaces

1 interface between chains.

A–B · 582 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

7NQD · Prim-Pol Domain of CRISPR-associated Prim-Pol (CAPP) from Marinitoga sp. 1137 · 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 H2J4R1
Elsewhere: RCSB PDB 7NQD · PDBe 7NQD · UniProt H2J4R1

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