Atomistry » Chlorine » PDB 3fee-3fpi » 3fl7
Atomistry »
  Chlorine »
    PDB 3fee-3fpi »
      3fl7 »

Chlorine in PDB 3fl7: Crystal Structure of the Human Ephrin A2 Ectodomain

Enzymatic activity of Crystal Structure of the Human Ephrin A2 Ectodomain

All present enzymatic activity of Crystal Structure of the Human Ephrin A2 Ectodomain:
2.7.10.1;

Protein crystallography data

The structure of Crystal Structure of the Human Ephrin A2 Ectodomain, PDB code: 3fl7 was solved by J.R.Walker, L.Yermekbayeva, A.Seitova, C.Butler-Cole, C.Bountra, J.Weigelt, C.H.Arrowsmith, A.M.Edwards, A.Bochkarev, S.Dhe-Paganon, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.59 / 2.50
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 59.358, 89.992, 136.476, 90.00, 90.00, 90.00
R / Rfree (%) 24.6 / 29.9

Other elements in 3fl7:

The structure of Crystal Structure of the Human Ephrin A2 Ectodomain also contains other interesting chemical elements:

Sodium (Na) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Human Ephrin A2 Ectodomain (pdb code 3fl7). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of the Human Ephrin A2 Ectodomain, PDB code: 3fl7:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in 3fl7

Go back to Chlorine Binding Sites List in 3fl7
Chlorine binding site 1 out of 3 in the Crystal Structure of the Human Ephrin A2 Ectodomain


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the Human Ephrin A2 Ectodomain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1002

b:83.3
occ:1.00
CB A:GLN56 3.9 64.5 1.0
N A:GLN56 4.5 63.0 1.0
OE1 A:GLN56 4.6 69.5 1.0
CE2 A:TYR65 4.6 60.9 1.0
CD A:GLN56 4.8 68.9 1.0
CD2 A:LEU54 4.8 53.1 1.0
CA A:GLN56 4.8 63.7 1.0
CG A:GLN56 4.9 66.8 1.0
CD2 A:TYR65 5.0 58.0 1.0

Chlorine binding site 2 out of 3 in 3fl7

Go back to Chlorine Binding Sites List in 3fl7
Chlorine binding site 2 out of 3 in the Crystal Structure of the Human Ephrin A2 Ectodomain


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of the Human Ephrin A2 Ectodomain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1003

b:75.5
occ:1.00
NH2 A:ARG486 3.3 54.9 1.0
CD A:LYS468 3.5 62.9 1.0
CE A:LYS468 3.7 63.1 1.0
CD A:ARG486 3.9 55.6 1.0
CZ A:ARG486 4.4 56.3 1.0
NZ A:LYS468 4.6 64.5 1.0
NE A:ARG486 4.6 55.4 1.0
CG A:LYS468 4.9 62.0 1.0
CB A:ARG486 5.0 53.0 1.0

Chlorine binding site 3 out of 3 in 3fl7

Go back to Chlorine Binding Sites List in 3fl7
Chlorine binding site 3 out of 3 in the Crystal Structure of the Human Ephrin A2 Ectodomain


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of the Human Ephrin A2 Ectodomain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1004

b:0.5
occ:1.00
O A:GLY171 3.5 64.7 1.0
N A:GLY171 3.6 61.0 1.0
CA A:VAL170 3.7 59.8 1.0
NH1 A:ARG93 3.7 59.1 1.0
O A:SER169 3.9 60.2 1.0
NH2 A:ARG93 4.1 61.7 1.0
C A:VAL170 4.1 60.4 1.0
CZ A:ARG93 4.4 61.0 1.0
CB A:VAL170 4.4 59.1 1.0
CG2 A:VAL170 4.4 60.2 1.0
C A:GLY171 4.5 64.2 1.0
N A:VAL170 4.6 59.0 1.0
C A:SER169 4.6 59.3 1.0
CA A:GLY171 4.6 62.6 1.0

Reference:

J.P.Himanen, L.Yermekbayeva, P.W.Janes, J.R.Walker, K.Xu, L.Atapattu, K.R.Rajashankar, A.Mensinga, M.Lackmann, D.B.Nikolov, S.Dhe-Paganon. Architecture of Eph Receptor Clusters. Proc.Natl.Acad.Sci.Usa V. 107 10860 2010.
ISSN: ISSN 0027-8424
PubMed: 20505120
DOI: 10.1073/PNAS.1004148107
Page generated: Sat Dec 12 09:42:06 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy