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PDBsum entry 5hez

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Top Page protein ligands metals Protein-protein interface(s) pores links
Pore analysis for: 5hez calculated with MOLE 2.0 PDB id
5hez
Pores calculated on whole structure Pores calculated excluding ligands

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9 pores, coloured by radius 11 pores, coloured by radius 11 pores, coloured as in
list below
Pores are connected internal spaces going through the structure. Only pores longer than 25 Å are shown.
Pores
Free R
Length
HPathy
HPhob
Polar
Rel Mut
Residue..type
Ligands
Radius
1 1.64 1.84 37.3 0.08 0.15 8.6 73 3 0 4 6 7 2 0  1M3 1203 A
2 1.95 2.15 45.1 -1.71 -0.36 25.0 75 8 5 1 2 1 2 0  PTR 1008 C 1M3 1201 C
3 2.32 2.36 45.8 -2.88 -0.55 36.7 80 11 5 2 2 0 1 0  PTR 1007 B PTR 1008 B PTR 1008 C
4 1.67 1.67 55.8 -2.53 -0.55 27.4 83 7 4 7 1 1 0 0  1M3 1203 D
5 2.34 4.53 56.0 -0.63 -0.02 17.4 73 7 3 2 6 6 2 0  1M3 1202 B CL 1201 D
6 1.35 1.36 63.7 -1.30 -0.26 14.9 77 6 4 4 4 4 3 0  PTR 1007 D PTR 1008 D 1M3 1202 D
7 1.95 2.14 67.7 -1.87 -0.49 24.0 81 10 7 7 3 1 2 0  1M3 1204 A PTR 1008 C 1M3 1201 C
8 2.04 2.22 75.1 -2.36 -0.53 31.9 77 13 7 5 2 1 2 0  PTR 1008 B 1M3 1203 B PTR 1008 C
9 1.34 1.31 90.7 -1.26 -0.12 16.6 75 8 3 8 8 9 5 0  1M3 1202 D
10 1.40 1.60 95.1 -0.93 -0.13 13.6 79 7 3 13 9 7 5 0  1M3 1202 B 1M3 1203 D
11 1.48 1.59 164.5 -1.18 -0.23 16.3 77 18 8 12 14 9 9 0  PTR 1007 B PTR 1008 B 1M3 1203 B 1M3 1202 D 1M3
1203 D

Residue-type_colouring
Positive Negative Neutral Aliphatic Aromatic Pro & Gly Cysteine
H,K,R D,E S,T,N,Q A,V,L,I,M F,Y,W P,G C

Acknowledgement
Pores were calculated by MOLE 2.0 program version 2.5.13.11.08 and visualized using Pymol 0.97rc.
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