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Crystal structure of CA2+-free prothrombin deletion mutant residues 146-167

Analyse Crystal structure of CA2+-free prothrombin deletion mutant residues 146-167 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4NZQ
Type: protein
Length: 508 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Prothrombin
EC: 3.4.21.5
UniProt: P00734
Ligands: NAG
Pockets: 7 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Prothrombin (EC 3.4.21.5)	protein	508	16% helix, 22% strand	P00734

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	826	0.71	0.77	72	empty
2	206	0.49	0.75	30	empty
3	123	0.48	0.79	27	empty
4	169	0.47	0.75	29	empty
5	130	0.46	0.78	32	empty

Modifications

Observed in the structure: 11 disulfide, 3 glycan (disulfide, N-glycosylation).

Compared structures

4NZQ · Crystal structure of Ca2+-free prothrombin deletion mutant residues 146-167 · 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 P00734
Elsewhere: RCSB PDB 4NZQ · PDBe 4NZQ · UniProt P00734

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