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Calcium in PDB 1r6v: Crystal Structure of Fervidolysin From Fervidobacterium Pennivorans, A Keratinolytic Enzyme Related to Subtilisin

Protein crystallography data

The structure of Crystal Structure of Fervidolysin From Fervidobacterium Pennivorans, A Keratinolytic Enzyme Related to Subtilisin, PDB code: 1r6v was solved by J.S.Kim, L.D.Kluskens, W.M.De Vos, R.Huber, J.Van Der Oost, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 1.70
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 49.558, 51.031, 79.101, 93.90, 104.72, 115.43
R / Rfree (%) 18.6 / 21.4

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Fervidolysin From Fervidobacterium Pennivorans, A Keratinolytic Enzyme Related to Subtilisin (pdb code 1r6v). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of Fervidolysin From Fervidobacterium Pennivorans, A Keratinolytic Enzyme Related to Subtilisin, PDB code: 1r6v:

Calcium binding site 1 out of 1 in 1r6v

Go back to Calcium Binding Sites List in 1r6v
Calcium binding site 1 out of 1 in the Crystal Structure of Fervidolysin From Fervidobacterium Pennivorans, A Keratinolytic Enzyme Related to Subtilisin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Fervidolysin From Fervidobacterium Pennivorans, A Keratinolytic Enzyme Related to Subtilisin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1

b:3.3
occ:1.00
O A:LYS223 2.3 19.8 1.0
O A:LYS219 2.3 18.2 1.0
OD1 A:ASP179 2.3 17.6 1.0
O A:ILE225 2.3 15.7 1.0
OE1 A:GLU137 2.4 22.6 1.0
OD1 A:ASP221 2.5 20.8 1.0
CG A:ASP179 3.4 16.8 1.0
C A:LYS223 3.5 19.9 1.0
C A:LYS219 3.5 18.3 1.0
CG A:ASP221 3.5 23.3 1.0
C A:ILE225 3.5 15.3 1.0
CD A:GLU137 3.6 21.1 1.0
OD2 A:ASP179 3.7 15.9 1.0
N A:ASP221 3.8 21.8 1.0
N A:ILE225 4.0 16.1 1.0
OD2 A:ASP221 4.1 23.1 1.0
N A:LYS223 4.1 19.8 1.0
C A:GLY224 4.2 17.1 1.0
CG A:GLU137 4.3 19.9 1.0
CA A:LYS223 4.3 20.2 1.0
CA A:ILE225 4.4 13.8 1.0
CA A:LYS219 4.4 18.2 1.0
N A:GLY224 4.4 19.9 1.0
N A:LYS220 4.4 20.0 1.0
CA A:LYS220 4.4 21.2 1.0
CA A:GLY224 4.5 17.2 1.0
N A:VAL226 4.5 15.0 1.0
N A:LYS219 4.5 15.9 1.0
OE2 A:GLU137 4.6 22.3 1.0
CA A:VAL226 4.6 13.3 1.0
C A:LYS220 4.6 21.2 1.0
CB A:ASP221 4.6 21.6 1.0
CA A:ASP221 4.6 22.7 1.0
N A:GLY222 4.7 21.2 1.0
O A:GLY224 4.7 17.5 1.0
CB A:LYS219 4.7 20.2 1.0
CB A:ASP179 4.7 16.8 1.0
CB A:GLU137 4.7 17.9 1.0
O A:HOH730 4.8 23.6 1.0
CB A:VAL226 4.8 14.7 1.0
C A:ASP221 4.8 22.7 1.0
CB A:LYS223 4.8 21.8 1.0
C A:ALA218 4.9 14.0 1.0

Reference:

J.S.Kim, L.D.Kluskens, W.M.De Vos, R.Huber, J.Van Der Oost. Crystal Structure of Fervidolysin From Fervidobacterium Pennivorans, A Keratinolytic Enzyme Related to Subtilisin. J.Mol.Biol. V. 335 787 2004.
ISSN: ISSN 0022-2836
PubMed: 14687574
DOI: 10.1016/J.JMB.2003.11.006
Page generated: Thu Jul 11 22:04:03 2024

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