Nickel in PDB 1slw: Rat Anionic N143H, E151H Trypsin Complexed to A86H Ecotin; Nickel- Bound

Enzymatic activity of Rat Anionic N143H, E151H Trypsin Complexed to A86H Ecotin; Nickel- Bound

All present enzymatic activity of Rat Anionic N143H, E151H Trypsin Complexed to A86H Ecotin; Nickel- Bound:
3.4.21.4;

Protein crystallography data

The structure of Rat Anionic N143H, E151H Trypsin Complexed to A86H Ecotin; Nickel- Bound, PDB code: 1slw was solved by L.S.Brinen, R.J.Fletterick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	6.00 / 2.00
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	86.380, 56.230, 81.230, 90.00, 92.81, 90.00
*R / R_free (%)*	17.9 / 25.3

Other elements in 1slw:

The structure of Rat Anionic N143H, E151H Trypsin Complexed to A86H Ecotin; Nickel- Bound also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

Nickel Binding Sites:

The binding sites of Nickel atom in the Rat Anionic N143H, E151H Trypsin Complexed to A86H Ecotin; Nickel- Bound (pdb code 1slw). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total only one binding site of Nickel was determined in the Rat Anionic N143H, E151H Trypsin Complexed to A86H Ecotin; Nickel- Bound, PDB code: 1slw:

Nickel binding site 1 out of 1 in 1slw

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Nickel Binding Sites List in 1slw

Nickel binding site 1 out of 1 in the Rat Anionic N143H, E151H Trypsin Complexed to A86H Ecotin; Nickel- Bound

Mono view

Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Rat Anionic N143H, E151H Trypsin Complexed to A86H Ecotin; Nickel- Bound within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Ni248 b:58.2 occ:1.00	NE2	A:HIS86	2.2	51.0	1.0
	NE2	B:HIS151	2.2	56.6	1.0
	O	B:HOH253	2.5	52.7	1.0
	NE2	B:HIS143	2.6	52.1	1.0
	CE1	A:HIS86	3.0	52.2	1.0
	CE1	B:HIS151	3.1	58.7	1.0
	CD2	A:HIS86	3.3	50.2	1.0
	CD2	B:HIS151	3.4	58.3	1.0
	CE1	B:HIS143	3.4	51.0	1.0
	CD2	B:HIS143	3.6	51.4	1.0
	ND1	A:HIS86	4.2	51.5	1.0
	ND1	B:HIS151	4.3	58.9	1.0
	CG	A:HIS86	4.4	51.7	1.0
	CG	B:HIS151	4.5	59.4	1.0
	ND1	B:HIS143	4.5	50.0	1.0
	CG	B:HIS143	4.7	48.9	1.0
	O	A:HOH143	4.8	45.7	1.0

Reference:

L.S.Brinen, W.S.Willett, C.S.Craik, R.J.Fletterick. X-Ray Structures of A Designed Binding Site in Trypsin Show Metal-Dependent Geometry. Biochemistry V. 35 5999 1996.
ISSN: ISSN 0006-2960
PubMed: 8634241
DOI: 10.1021/BI9530200

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