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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

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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

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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: Wed Dec 16 04:51:25 2020

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