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Lead in PDB 1ka4: Structure of Pyrococcus Furiosus Carboxypeptidase Nat-Pb

Protein crystallography data

The structure of Structure of Pyrococcus Furiosus Carboxypeptidase Nat-Pb, PDB code: 1ka4 was solved by J.W.Arndt, B.Hao, V.Ramakrishnan, T.Cheng, S.I.Chan, M.K.Chan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.75 / 3.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 132.300, 67.582, 67.185, 90.00, 95.20, 90.00
R / Rfree (%) 23.6 / 27.6

Lead Binding Sites:

The binding sites of Lead atom in the Structure of Pyrococcus Furiosus Carboxypeptidase Nat-Pb (pdb code 1ka4). This binding sites where shown within 5.0 Angstroms radius around Lead atom.
In total only one binding site of Lead was determined in the Structure of Pyrococcus Furiosus Carboxypeptidase Nat-Pb, PDB code: 1ka4:

Lead binding site 1 out of 1 in 1ka4

Go back to Lead Binding Sites List in 1ka4
Lead binding site 1 out of 1 in the Structure of Pyrococcus Furiosus Carboxypeptidase Nat-Pb


Mono view


Stereo pair view

A full contact list of Lead with other atoms in the Pb binding site number 1 of Structure of Pyrococcus Furiosus Carboxypeptidase Nat-Pb within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Pb601

b:36.0
occ:1.00
OE2 A:GLU299 1.9 51.9 1.0
NE2 A:HIS273 2.0 49.4 1.0
O A:HOH602 2.2 37.8 1.0
NE2 A:HIS269 2.3 45.7 1.0
CE1 A:HIS273 2.9 48.9 1.0
CD2 A:HIS273 3.0 49.9 1.0
CD A:GLU299 3.1 51.2 1.0
CD2 A:HIS269 3.2 42.8 1.0
CE1 A:HIS269 3.3 44.9 1.0
OG A:SER302 3.6 39.5 1.0
OE1 A:GLU299 3.7 51.3 1.0
ND1 A:HIS273 4.0 49.7 1.0
CG A:HIS273 4.1 47.8 1.0
CB A:SER302 4.1 39.3 1.0
OE2 A:GLU270 4.2 41.2 1.0
CG A:GLU299 4.3 47.4 1.0
O A:HOH608 4.3 29.3 1.0
ND1 A:HIS269 4.3 44.3 1.0
CG A:HIS269 4.3 41.6 1.0
OE1 A:GLU270 4.6 39.6 1.0
O A:HOH658 4.6 35.6 1.0
CD A:GLU270 4.8 40.2 1.0

Reference:

J.W.Arndt, B.Hao, V.Ramakrishnan, T.Cheng, S.I.Chan, M.K.Chan. Crystal Structure of A Novel Carboxypeptidase From the Hyperthermophilic Archaeon Pyrococcus Furiosus Structure V. 10 215 2002.
ISSN: ISSN 0969-2126
PubMed: 11839307
DOI: 10.1016/S0969-2126(02)00698-6
Page generated: Wed Dec 16 02:01:56 2020

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