Atomistry » Zinc » PDB 3sud-3t5z » 3t3w
Atomistry »
  Zinc »
    PDB 3sud-3t5z »
      3t3w »

Zinc in PDB 3t3w: Crystal Structure of Probable Enoyl-Coa Hydratase From Mycobacterium Thermoresistibile

Enzymatic activity of Crystal Structure of Probable Enoyl-Coa Hydratase From Mycobacterium Thermoresistibile

All present enzymatic activity of Crystal Structure of Probable Enoyl-Coa Hydratase From Mycobacterium Thermoresistibile:
4.2.1.17;

Protein crystallography data

The structure of Crystal Structure of Probable Enoyl-Coa Hydratase From Mycobacterium Thermoresistibile, PDB code: 3t3w was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.22 / 1.80
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 124.240, 124.240, 212.250, 90.00, 90.00, 90.00
R / Rfree (%) 13.9 / 16.5

Other elements in 3t3w:

The structure of Crystal Structure of Probable Enoyl-Coa Hydratase From Mycobacterium Thermoresistibile also contains other interesting chemical elements:

Iodine (I) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Probable Enoyl-Coa Hydratase From Mycobacterium Thermoresistibile (pdb code 3t3w). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the Crystal Structure of Probable Enoyl-Coa Hydratase From Mycobacterium Thermoresistibile, PDB code: 3t3w:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in 3t3w

Go back to Zinc Binding Sites List in 3t3w
Zinc binding site 1 out of 6 in the Crystal Structure of Probable Enoyl-Coa Hydratase From Mycobacterium Thermoresistibile


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Probable Enoyl-Coa Hydratase From Mycobacterium Thermoresistibile within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:18.6
occ:1.00
NE2 A:HIS249 2.0 14.3 1.0
NE2 A:HIS253 2.1 18.0 1.0
O A:HOH280 2.1 16.4 1.0
OE2 A:GLU160 2.1 16.1 1.0
OE2 A:GLU99 2.1 16.5 1.0
OE1 A:GLU99 2.2 16.6 1.0
CD A:GLU99 2.4 16.3 1.0
CE1 A:HIS249 3.0 15.1 1.0
CE1 A:HIS253 3.0 20.3 1.0
CD2 A:HIS249 3.1 14.1 1.0
CD2 A:HIS253 3.1 19.2 1.0
CD A:GLU160 3.1 16.6 1.0
CG A:GLU160 3.7 15.4 1.0
O A:HOH718 3.9 28.4 1.0
CG A:GLU99 3.9 16.8 1.0
O A:HOH300 4.0 19.5 1.0
O A:HOH631 4.1 36.0 1.0
OE1 A:GLU160 4.1 15.7 1.0
ND1 A:HIS253 4.2 20.6 1.0
ND1 A:HIS249 4.2 14.7 1.0
CG A:HIS249 4.2 13.2 1.0
CG A:HIS253 4.2 19.8 1.0
NE2 A:GLN250 4.4 16.7 1.0
O A:HOH453 4.5 27.1 1.0
CB A:GLU99 4.7 16.2 1.0
CE2 A:TYR103 4.9 18.3 1.0
CD2 A:TYR103 4.9 17.4 1.0

Zinc binding site 2 out of 6 in 3t3w

Go back to Zinc Binding Sites List in 3t3w
Zinc binding site 2 out of 6 in the Crystal Structure of Probable Enoyl-Coa Hydratase From Mycobacterium Thermoresistibile


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Probable Enoyl-Coa Hydratase From Mycobacterium Thermoresistibile within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn301

b:18.3
occ:1.00
NE2 B:HIS249 2.0 14.1 1.0
NE2 B:HIS253 2.1 18.4 1.0
OE2 B:GLU160 2.1 17.1 1.0
OE2 B:GLU99 2.1 16.4 1.0
O B:HOH277 2.2 16.3 1.0
OE1 B:GLU99 2.2 17.3 1.0
CD B:GLU99 2.5 15.9 1.0
CE1 B:HIS249 3.0 14.9 1.0
CD2 B:HIS249 3.0 14.7 1.0
CE1 B:HIS253 3.0 20.5 1.0
CD2 B:HIS253 3.1 19.6 1.0
CD B:GLU160 3.1 17.0 1.0
CG B:GLU160 3.6 16.4 1.0
O B:HOH766 3.9 25.5 1.0
CG B:GLU99 4.0 15.7 1.0
O B:HOH423 4.1 22.6 1.0
OE1 B:GLU160 4.1 16.5 1.0
O B:HOH1283 4.1 37.0 1.0
ND1 B:HIS249 4.2 14.9 1.0
ND1 B:HIS253 4.2 20.2 1.0
CG B:HIS249 4.2 14.3 1.0
CG B:HIS253 4.2 19.5 1.0
NE2 B:GLN250 4.4 17.3 1.0
O B:HOH389 4.5 26.6 1.0
CB B:GLU99 4.7 15.3 1.0
CD2 B:TYR103 4.9 19.6 1.0
CE2 B:TYR103 4.9 20.3 1.0

Zinc binding site 3 out of 6 in 3t3w

Go back to Zinc Binding Sites List in 3t3w
Zinc binding site 3 out of 6 in the Crystal Structure of Probable Enoyl-Coa Hydratase From Mycobacterium Thermoresistibile


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Probable Enoyl-Coa Hydratase From Mycobacterium Thermoresistibile within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn301

b:11.8
occ:1.00
NE2 C:HIS253 2.1 11.1 1.0
NE2 C:HIS249 2.1 9.1 1.0
OE2 C:GLU160 2.1 9.7 1.0
OE2 C:GLU99 2.2 10.9 1.0
O C:HOH277 2.2 12.3 1.0
OE1 C:GLU99 2.2 10.0 1.0
CD C:GLU99 2.5 10.6 1.0
CE1 C:HIS253 3.0 12.4 1.0
CD2 C:HIS249 3.1 8.7 1.0
CD C:GLU160 3.1 10.0 1.0
CE1 C:HIS249 3.1 8.9 1.0
CD2 C:HIS253 3.1 11.1 1.0
CG C:GLU160 3.6 10.1 1.0
O C:HOH329 3.8 19.7 1.0
CG C:GLU99 4.0 10.4 1.0
O C:HOH284 4.0 13.2 1.0
OE1 C:GLU160 4.1 10.7 1.0
O C:HOH536 4.1 26.4 1.0
ND1 C:HIS253 4.2 11.7 1.0
CG C:HIS249 4.2 8.2 1.0
ND1 C:HIS249 4.2 8.4 1.0
CG C:HIS253 4.3 10.8 1.0
NE2 C:GLN250 4.4 10.3 1.0
O C:HOH321 4.6 19.0 1.0
CB C:GLU99 4.7 10.3 1.0
CD2 C:TYR103 4.9 12.5 1.0
CE2 C:TYR103 4.9 13.1 1.0

Zinc binding site 4 out of 6 in 3t3w

Go back to Zinc Binding Sites List in 3t3w
Zinc binding site 4 out of 6 in the Crystal Structure of Probable Enoyl-Coa Hydratase From Mycobacterium Thermoresistibile


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Probable Enoyl-Coa Hydratase From Mycobacterium Thermoresistibile within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn301

b:10.6
occ:1.00
NE2 D:HIS249 2.1 7.7 1.0
OE2 D:GLU160 2.1 9.0 1.0
NE2 D:HIS253 2.1 8.9 1.0
OE2 D:GLU99 2.1 8.6 1.0
O D:HOH871 2.1 8.3 1.0
OE1 D:GLU99 2.2 9.0 1.0
CD D:GLU99 2.4 9.0 1.0
CE1 D:HIS253 3.0 9.3 1.0
CD2 D:HIS249 3.1 7.6 1.0
CE1 D:HIS249 3.1 8.1 1.0
CD D:GLU160 3.1 9.0 1.0
CD2 D:HIS253 3.1 8.7 1.0
CG D:GLU160 3.6 8.7 1.0
O D:HOH320 3.8 13.6 1.0
CG D:GLU99 4.0 9.3 1.0
O D:HOH290 4.0 9.8 1.0
O D:HOH817 4.0 21.8 1.0
OE1 D:GLU160 4.1 9.2 1.0
ND1 D:HIS249 4.2 7.8 1.0
ND1 D:HIS253 4.2 9.4 1.0
CG D:HIS249 4.2 7.7 1.0
CG D:HIS253 4.3 9.2 1.0
NE2 D:GLN250 4.4 9.9 1.0
O D:HOH321 4.5 24.6 1.0
CB D:GLU99 4.7 9.2 1.0
CD2 D:TYR103 4.9 11.0 1.0
CE2 D:TYR103 4.9 11.5 1.0

Zinc binding site 5 out of 6 in 3t3w

Go back to Zinc Binding Sites List in 3t3w
Zinc binding site 5 out of 6 in the Crystal Structure of Probable Enoyl-Coa Hydratase From Mycobacterium Thermoresistibile


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Crystal Structure of Probable Enoyl-Coa Hydratase From Mycobacterium Thermoresistibile within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Zn301

b:10.3
occ:1.00
NE2 E:HIS249 2.1 7.2 1.0
NE2 E:HIS253 2.1 10.1 1.0
OE2 E:GLU160 2.1 8.6 1.0
OE2 E:GLU99 2.1 8.7 1.0
O E:HOH872 2.1 9.0 1.0
OE1 E:GLU99 2.2 9.4 1.0
CD E:GLU99 2.4 9.0 1.0
CE1 E:HIS249 3.0 7.3 1.0
CD2 E:HIS249 3.1 7.2 1.0
CE1 E:HIS253 3.1 10.3 1.0
CD2 E:HIS253 3.1 9.8 1.0
CD E:GLU160 3.1 8.0 1.0
CG E:GLU160 3.6 7.9 1.0
O E:HOH421 3.8 17.8 1.0
CG E:GLU99 3.9 9.2 1.0
O E:HOH307 4.0 10.9 1.0
OE1 E:GLU160 4.1 8.1 1.0
ND1 E:HIS249 4.2 7.1 1.0
O E:HOH711 4.2 32.8 1.0
CG E:HIS249 4.2 7.0 1.0
ND1 E:HIS253 4.2 10.6 1.0
CG E:HIS253 4.2 9.8 1.0
NE2 E:GLN250 4.4 9.0 1.0
O E:HOH328 4.6 19.5 1.0
CB E:GLU99 4.7 8.8 1.0
CD2 E:TYR103 4.9 9.4 1.0
CE2 E:TYR103 5.0 9.8 1.0

Zinc binding site 6 out of 6 in 3t3w

Go back to Zinc Binding Sites List in 3t3w
Zinc binding site 6 out of 6 in the Crystal Structure of Probable Enoyl-Coa Hydratase From Mycobacterium Thermoresistibile


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Crystal Structure of Probable Enoyl-Coa Hydratase From Mycobacterium Thermoresistibile within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Zn301

b:11.0
occ:1.00
NE2 F:HIS249 2.1 8.1 1.0
NE2 F:HIS253 2.1 10.7 1.0
O F:HOH277 2.1 11.4 1.0
OE2 F:GLU99 2.1 9.1 1.0
OE2 F:GLU160 2.1 9.2 1.0
OE1 F:GLU99 2.2 9.3 1.0
CD F:GLU99 2.5 9.4 1.0
CE1 F:HIS253 3.0 12.1 1.0
CD2 F:HIS249 3.0 8.0 1.0
CE1 F:HIS249 3.1 8.2 1.0
CD F:GLU160 3.1 9.2 1.0
CD2 F:HIS253 3.2 10.4 1.0
CG F:GLU160 3.6 8.8 1.0
O F:HOH282 3.8 16.6 1.0
CG F:GLU99 4.0 9.6 1.0
O F:HOH284 4.0 11.6 1.0
O F:HOH658 4.1 32.7 1.0
OE1 F:GLU160 4.1 9.6 1.0
ND1 F:HIS253 4.2 11.8 1.0
ND1 F:HIS249 4.2 7.9 1.0
CG F:HIS249 4.2 7.9 1.0
CG F:HIS253 4.3 10.9 1.0
NE2 F:GLN250 4.4 10.4 1.0
O F:HOH398 4.5 17.9 1.0
CB F:GLU99 4.7 9.8 1.0
CD2 F:TYR103 4.9 10.7 1.0
CE2 F:TYR103 4.9 11.2 1.0

Reference:

L.Baugh, I.Phan, D.W.Begley, M.C.Clifton, B.Armour, D.M.Dranow, B.M.Taylor, M.M.Muruthi, J.Abendroth, J.W.Fairman, D.Fox, S.H.Dieterich, B.L.Staker, A.S.Gardberg, R.Choi, S.N.Hewitt, A.J.Napuli, J.Myers, L.K.Barrett, Y.Zhang, M.Ferrell, E.Mundt, K.Thompkins, N.Tran, S.Lyons-Abbott, A.Abramov, A.Sekar, D.Serbzhinskiy, D.Lorimer, G.W.Buchko, R.Stacy, L.J.Stewart, T.E.Edwards, W.C.Van Voorhis, P.J.Myler. Increasing the Structural Coverage of Tuberculosis Drug Targets. Tuberculosis (Edinb) V. 95 142 2015.
ISSN: ISSN 1472-9792
PubMed: 25613812
DOI: 10.1016/J.TUBE.2014.12.003
Page generated: Sat Oct 26 16:18:51 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy