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Zinc in PDB 2jih: Crystal Structure of Human Adamts-1 Catalytic Domain and Cysteine- Rich Domain (Complex-Form)

Protein crystallography data

The structure of Crystal Structure of Human Adamts-1 Catalytic Domain and Cysteine- Rich Domain (Complex-Form), PDB code: 2jih was solved by S.Gerhardt, G.Hassall, P.Hawtin, E.Mccall, L.Flavell, C.Minshull, D.Hargreaves, A.Ting, R.A.Pauptit, A.E.Parker, W.M.Abbott, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 56.90 / 2.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 51.579, 64.396, 113.524, 90.00, 90.91, 90.00
R / Rfree (%) 22.4 / 28.2

Other elements in 2jih:

The structure of Crystal Structure of Human Adamts-1 Catalytic Domain and Cysteine- Rich Domain (Complex-Form) also contains other interesting chemical elements:

Nickel (Ni) 12 atoms
Magnesium (Mg) 6 atoms
Cadmium (Cd) 6 atoms
Sodium (Na) 5 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Human Adamts-1 Catalytic Domain and Cysteine- Rich Domain (Complex-Form) (pdb code 2jih). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Human Adamts-1 Catalytic Domain and Cysteine- Rich Domain (Complex-Form), PDB code: 2jih:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2jih

Go back to Zinc Binding Sites List in 2jih
Zinc binding site 1 out of 2 in the Crystal Structure of Human Adamts-1 Catalytic Domain and Cysteine- Rich Domain (Complex-Form)


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 Human Adamts-1 Catalytic Domain and Cysteine- Rich Domain (Complex-Form) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1553

b:29.1
occ:1.00
O4 A:0971001 2.1 43.4 1.0
NE2 A:HIS401 2.2 31.9 1.0
NE2 A:HIS411 2.2 37.4 1.0
NE2 A:HIS405 2.3 31.5 1.0
O3 A:0971001 2.4 46.9 1.0
C12 A:0971001 2.8 45.0 1.0
N3 A:0971001 3.0 45.5 1.0
CE1 A:HIS401 3.1 33.4 1.0
CE1 A:HIS411 3.1 35.5 1.0
CE1 A:HIS405 3.1 31.0 1.0
CD2 A:HIS411 3.2 36.5 1.0
CD2 A:HIS401 3.2 32.0 1.0
CD2 A:HIS405 3.4 29.5 1.0
O A:HOH2122 4.2 26.0 1.0
ND1 A:HIS401 4.2 32.5 1.0
ND1 A:HIS411 4.2 35.0 1.0
C13 A:0971001 4.2 43.3 1.0
CG A:HIS411 4.3 35.1 1.0
ND1 A:HIS405 4.3 33.6 1.0
CG A:HIS401 4.3 32.0 1.0
OE1 A:GLU402 4.4 32.4 1.0
CG A:HIS405 4.4 31.8 1.0
C14 A:0971001 4.6 43.2 1.0
C15 A:0971001 4.7 42.2 1.0
O A:HOH2066 4.8 34.8 1.0
CE A:MET430 4.8 32.8 1.0
OE2 A:GLU402 4.9 30.3 1.0
O5 A:0971001 5.0 44.3 1.0

Zinc binding site 2 out of 2 in 2jih

Go back to Zinc Binding Sites List in 2jih
Zinc binding site 2 out of 2 in the Crystal Structure of Human Adamts-1 Catalytic Domain and Cysteine- Rich Domain (Complex-Form)


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 Human Adamts-1 Catalytic Domain and Cysteine- Rich Domain (Complex-Form) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1554

b:29.2
occ:1.00
O4 B:0971001 2.1 45.9 1.0
NE2 B:HIS401 2.1 28.1 1.0
NE2 B:HIS405 2.2 33.0 1.0
NE2 B:HIS411 2.2 34.7 1.0
O3 B:0971001 2.3 46.0 1.0
C12 B:0971001 2.8 45.9 1.0
N3 B:0971001 2.9 46.6 1.0
CD2 B:HIS401 3.1 30.1 1.0
CD2 B:HIS411 3.1 35.7 1.0
CE1 B:HIS401 3.1 31.2 1.0
CD2 B:HIS405 3.1 33.4 1.0
CE1 B:HIS405 3.2 34.0 1.0
CE1 B:HIS411 3.2 36.0 1.0
ND1 B:HIS401 4.2 27.8 1.0
CG B:HIS401 4.2 30.8 1.0
CG B:HIS411 4.2 35.7 1.0
C13 B:0971001 4.3 43.6 1.0
ND1 B:HIS411 4.3 34.5 1.0
ND1 B:HIS405 4.3 34.7 1.0
CG B:HIS405 4.3 32.4 1.0
O B:HOH2088 4.3 31.8 1.0
OE1 B:GLU402 4.4 32.6 1.0
C15 B:0971001 4.7 40.5 1.0
C14 B:0971001 4.7 42.4 1.0
CE B:MET430 4.8 37.2 1.0
OE2 B:GLU402 4.8 33.2 1.0
O5 B:0971001 4.8 43.7 1.0
O B:HOH2087 4.8 32.1 1.0
CD B:GLU402 5.0 32.8 1.0

Reference:

S.Gerhardt, G.Hassall, P.Hawtin, E.Mccall, L.Flavell, C.Minshull, D.Hargreaves, A.Ting, R.A.Pauptit, A.E.Parker, W.M.Abbott. Crystal Structures of Human Adamts-1 Reveal A Conserved Catalytic Domain and A Disintegrin-Like Domain with A Fold Homologous to Cysteine-Rich Domains. J. Mol. Biol. V. 373 891 2007.
ISSN: ISSN 0022-2836
PubMed: 17897672
DOI: 10.1016/J.JMB.2007.07.047
Page generated: Wed Dec 16 03:32:02 2020

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