Zinc in PDB 3mtw: Crystal Structure of L-Lysine, L-Arginine Carboxypeptidase CC2672 From Caulobacter Crescentus CB15 Complexed with N-Methyl Phosphonate Derivative of L-Arginine

The structure of Crystal Structure of L-Lysine, L-Arginine Carboxypeptidase CC2672 From Caulobacter Crescentus CB15 Complexed with N-Methyl Phosphonate Derivative of L-Arginine, PDB code: 3mtw was solved by A.A.Fedorov, E.V.Fedorov, D.F.Xiang, F.M.Raushel, S.C.Almo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.35 / 1.70
Space group	I 4 3 2
Cell size a, b, c (Å), α, β, γ (°)	200.315, 200.315, 200.315, 90.00, 90.00, 90.00
R / Rfree (%)	18 / 20.3

The binding sites of Zinc atom in the Crystal Structure of L-Lysine, L-Arginine Carboxypeptidase CC2672 From Caulobacter Crescentus CB15 Complexed with N-Methyl Phosphonate Derivative of L-Arginine (pdb code 3mtw). 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 L-Lysine, L-Arginine Carboxypeptidase CC2672 From Caulobacter Crescentus CB15 Complexed with N-Methyl Phosphonate Derivative of L-Arginine, PDB code: 3mtw:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of L-Lysine, L-Arginine Carboxypeptidase CC2672 From Caulobacter Crescentus CB15 Complexed with N-Methyl Phosphonate Derivative of L-Arginine


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 L-Lysine, L-Arginine Carboxypeptidase CC2672 From Caulobacter Crescentus CB15 Complexed with N-Methyl Phosphonate Derivative of L-Arginine within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1 b:18.0 occ:1.00 OPA A:M3R430 2.0 18.9 1.0 NE2 A:HIS92 2.0 13.9 1.0 OQ1 A:KCX211 2.0 19.1 1.0 NE2 A:HIS90 2.1 14.7 1.0 OD1 A:ASP344 2.4 16.6 1.0 CE1 A:HIS92 3.0 17.7 1.0 CD2 A:HIS90 3.0 17.6 1.0 CD2 A:HIS92 3.0 14.2 1.0 CX A:KCX211 3.1 16.2 1.0 CE1 A:HIS90 3.1 15.7 1.0 P A:M3R430 3.2 18.5 1.0 CG A:ASP344 3.2 18.6 1.0 OD2 A:ASP344 3.4 18.0 1.0 CP A:M3R430 3.5 19.1 1.0 OQ2 A:KCX211 3.6 14.0 1.0 OPB A:M3R430 3.8 17.1 1.0 ZN A:ZN2 4.0 18.3 1.0 NZ A:KCX211 4.0 16.4 1.0 ND1 A:HIS92 4.1 19.6 1.0 CG2 A:VAL134 4.1 16.7 1.0 CG A:HIS90 4.2 16.9 1.0 ND1 A:HIS90 4.2 16.9 1.0 CG A:HIS92 4.2 17.4 1.0 N A:M3R430 4.4 21.0 1.0 CB A:ASP344 4.6 16.9 1.0 CE1 A:HIS272 4.6 18.7 1.0 NE2 A:HIS272 4.6 17.0 1.0 O A:HOH516 4.7 32.8 1.0 O A:VAL134 4.9 17.3 1.0 O A:HOH724 4.9 29.6 1.0 CA A:ASP344 4.9 16.4 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of L-Lysine, L-Arginine Carboxypeptidase CC2672 From Caulobacter Crescentus CB15 Complexed with N-Methyl Phosphonate Derivative of L-Arginine


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 L-Lysine, L-Arginine Carboxypeptidase CC2672 From Caulobacter Crescentus CB15 Complexed with N-Methyl Phosphonate Derivative of L-Arginine within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2 b:18.3 occ:1.00 OPB A:M3R430 1.9 17.1 1.0 OQ2 A:KCX211 2.0 14.0 1.0 NE2 A:HIS272 2.1 17.0 1.0 ND1 A:HIS252 2.1 18.0 1.0 CD2 A:HIS272 2.9 16.8 1.0 CX A:KCX211 3.0 16.2 1.0 CE1 A:HIS252 3.0 18.5 1.0 P A:M3R430 3.0 18.5 1.0 OPA A:M3R430 3.1 18.9 1.0 CG A:HIS252 3.2 18.5 1.0 CE1 A:HIS272 3.2 18.7 1.0 OQ1 A:KCX211 3.2 19.1 1.0 CB A:HIS252 3.5 17.3 1.0 O A:HOH516 3.6 32.8 1.0 ZN A:ZN1 4.0 18.0 1.0 CA A:M3R430 4.0 26.4 1.0 NE2 A:HIS171 4.0 21.4 1.0 N A:M3R430 4.0 21.0 1.0 NZ A:KCX211 4.1 16.4 1.0 CG A:HIS272 4.2 16.3 1.0 NE2 A:HIS252 4.2 18.4 1.0 ND1 A:HIS272 4.2 15.1 1.0 CD2 A:HIS252 4.2 20.9 1.0 CE1 A:HIS90 4.3 15.7 1.0 CP A:M3R430 4.3 19.1 1.0 CD2 A:HIS171 4.4 19.5 1.0 CA A:HIS252 4.4 17.9 1.0 O A:M3R430 4.5 15.6 1.0 NE2 A:HIS90 4.5 14.7 1.0 C A:M3R430 4.5 23.8 1.0 CE A:KCX211 4.6 17.4 1.0 OD2 A:ASP344 4.9 18.0 1.0

D.F.Xiang, Y.Patskovsky, C.Xu, A.A.Fedorov, E.V.Fedorov, A.A.Sisco, J.M.Sauder, S.K.Burley, S.C.Almo, F.M.Raushel. Functional Identification and Structure Determination of Two Novel Prolidases From COG1228 in the Amidohydrolase Superfamily Biochemistry V. 49 6791 2010.
ISSN: ISSN 0006-2960
PubMed: 20604542
DOI: 10.1021/BI100897U