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Apo enzyme of human polymerase lambda

Analyse Apo enzyme of human polymerase lambda in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5CB1
Type: protein
Length: 571 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA polymerase lambda
EC: 2.7.7.7
UniProt: Q9UGP5
Pockets: 4 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA polymerase lambda (EC 2.7.7.7)	protein	326	48% helix, 15% strand	Q9UGP5
B	DNA polymerase lambda (EC 2.7.7.7)	protein	245	41% helix, 16% strand	Q9UGP5

Pockets

4 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	96	0.68	0.92	19	empty
2	748	0.67	0.75	52	empty
3	322	0.56	0.76	34	empty
4	62	0.28	0.73	20	empty

Interfaces

1 interface between chains.

A–B · 629 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

5CB1 · Apo enzyme of human Polymerase lambda · the same entry in another collection · chain A against A, TM-score 1.00
Q9UGP5 · AlphaFold monomer V2.0 prediction for DNA polymerase lambda (Q9UGP5) · a predicted model of the same protein · chain B against A, TM-score 0.92

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 Q9UGP5
Elsewhere: RCSB PDB 5CB1 · PDBe 5CB1 · UniProt Q9UGP5

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