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Iron in PDB 4fwy: F33Y Cub Myoglobin (F33Y L29H F43H Sperm Whale Myoglobin) with Copper Bound

Protein crystallography data

The structure of F33Y Cub Myoglobin (F33Y L29H F43H Sperm Whale Myoglobin) with Copper Bound, PDB code: 4fwy was solved by Y.-G.Gao, H.Robinson, I.D.Petrik, K.D.Miner, Y.Lu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.01 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 39.734, 48.286, 77.691, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 24.6

Other elements in 4fwy:

The structure of F33Y Cub Myoglobin (F33Y L29H F43H Sperm Whale Myoglobin) with Copper Bound also contains other interesting chemical elements:

Copper (Cu) 5 atoms

Iron Binding Sites:

The binding sites of Iron atom in the F33Y Cub Myoglobin (F33Y L29H F43H Sperm Whale Myoglobin) with Copper Bound (pdb code 4fwy). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the F33Y Cub Myoglobin (F33Y L29H F43H Sperm Whale Myoglobin) with Copper Bound, PDB code: 4fwy:

Iron binding site 1 out of 1 in 4fwy

Go back to Iron Binding Sites List in 4fwy
Iron binding site 1 out of 1 in the F33Y Cub Myoglobin (F33Y L29H F43H Sperm Whale Myoglobin) with Copper Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of F33Y Cub Myoglobin (F33Y L29H F43H Sperm Whale Myoglobin) with Copper Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe201

b:27.1
occ:1.00
FE A:HEM201 0.0 27.1 1.0
NA A:HEM201 1.9 27.1 1.0
NC A:HEM201 2.0 27.4 1.0
NE2 A:HIS93 2.1 27.0 1.0
NB A:HEM201 2.1 25.1 1.0
ND A:HEM201 2.1 28.1 1.0
O A:HOH342 2.5 33.3 1.0
C4A A:HEM201 3.0 27.6 1.0
CE1 A:HIS93 3.0 32.2 1.0
C4B A:HEM201 3.0 25.2 1.0
CD2 A:HIS93 3.1 27.0 1.0
C1C A:HEM201 3.1 27.5 1.0
C1B A:HEM201 3.1 24.9 1.0
C4C A:HEM201 3.1 29.6 1.0
C1D A:HEM201 3.1 31.6 1.0
C1A A:HEM201 3.1 27.4 1.0
C4D A:HEM201 3.1 31.5 1.0
CHC A:HEM201 3.5 24.9 1.0
CHB A:HEM201 3.5 26.7 1.0
CHD A:HEM201 3.5 30.2 1.0
CHA A:HEM201 3.6 29.3 1.0
ND1 A:HIS93 4.2 28.2 1.0
CG A:HIS93 4.2 27.1 1.0
C3A A:HEM201 4.3 26.8 1.0
C3C A:HEM201 4.4 30.4 1.0
C3B A:HEM201 4.4 24.9 1.0
C2A A:HEM201 4.4 28.8 1.0
C2C A:HEM201 4.4 27.9 1.0
C2B A:HEM201 4.4 23.9 1.0
C3D A:HEM201 4.4 34.9 1.0
C2D A:HEM201 4.5 35.3 1.0
CG2 A:VAL68 4.6 25.2 1.0
CE1 A:HIS64 4.8 30.0 1.0
NE2 A:HIS43 4.8 78.8 1.0

Reference:

K.D.Miner, A.Mukherjee, Y.G.Gao, E.L.Null, I.D.Petrik, X.Zhao, N.Yeung, H.Robinson, Y.Lu. A Designed Functional Metalloenzyme That Reduces O(2) to H(2) O with Over One Thousand Turnovers. Angew.Chem.Int.Ed.Engl. V. 51 5589 2012.
ISSN: ISSN 1433-7851
PubMed: 22539151
DOI: 10.1002/ANIE.201201981
Page generated: Mon Aug 5 02:29:59 2024

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