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Proteins in PDB homologous to 1pfqA

36 proteins (294 PDB structures) with E() < 0.001

Homologs in SwissProt


Acc   E.C. E() % id alen 547
&Y
630
*S
631
%Y
708
&D
740
*H
1n1mA, 1n1mB, 1nu6A, 1nu6B, 1nu8A, 1nu8B, 1tk3A, 1tk3B, 1tkrA, 1tkrB, 1w1iA, 1w1iB, 1w1iC, 1w1iD, 1rwqA, 1rwqB, 2bgnA, 2bgnB, 2bgnC, 2bgnD, 2ajlI, 2ajlJ, 2bubA, 2bubB, 2ogzA, 2ogzB, 2oqiA, 2oqiB, 2oqiC, 2oqiD, 2oleA, 2oleB, 3bjmA, 3bjmB, 3eioA, 3eioB, 3h0cA, 3h0cB, 3kwfA, 3kwfB, 3oc0A, 3oc0B, 3kwjA, 3kwjB, 4dsaA, 4dsaB, 4dszA, 4dszB, 4dtcA, 4dtcBHuman Dipeptidyl Peptidase IvCD26 IN COM3.4.14.50100.0728 &Y*S%Y&D*H
2ripADppiv In Complex With An Inhibitor3.4.14.50100.0728 &Y*S%Y&D*H
1pfqA, 1pfqBHuman Apo Dipeptidyl Peptidase Iv / Cd263.4.14.50100.0728 &Y*S%Y&D*H
1r9mA, 1r9mB, 1r9mC, 1r9mDHuman Dipeptidyl Peptidase Iv At 2.1 Ang3.4.14.50100.0728 &Y*S%Y&D*H
2rguA, 2rguBComplex Of Human Dpp4 And Inhibitor3.4.14.50100.0728 &Y*S%Y&D*H
2jidA, 2jidBHuman Dipeptidyl Peptidase Iv In Complex3.4.14.50100.0728 &Y*S%Y&D*H
2bgrA, 2bgrBHiv-1 Tat Derived Nonapeptides Tat(1-9) 3.4.14.50100.0728 &Y*S%Y&D*H
1r9nA, 1r9nB, 1r9nC, 1r9nDHuman Dipeptidyl Peptidase Iv In Complex3.4.14.50100.0728 &Y*S%Y&D*H
3ccbA, 3ccbB, 3ccbC, 3ccbD, 3cccA, 3cccB, 3cccC, 3cccD, 3g0bA, 3g0bB, 3g0bC, 3g0bD, 3g0cA, 3g0cB, 3g0cC, 3g0cD, 3g0dA, 3g0dB, 3g0dC, 3g0dD, 3g0gA, 3g0gB, 3g0gC, 3g0gD, 3o95A, 3o95B, 3o95C, 3o95D, 3o9vA, 3o9vB, 3o9vC, 3o9vD, 3opmA, 3opmB, 3opmC, 3opmD, 4g1fA, 4g1fB, 4g1fC, 4g1fDHuman Dpp4 In Complex With A Benzimidazo3.4.14.50100.0728 &Y*S%Y&D*H
1j2eA, 1j2eB, 1wcyA, 1wcyB, 3vjmA, 3vjmB, 3vjkA, 3vjkB, 3vjlA, 3vjlB, 3w2tA, 3w2tBHuman Dipeptidyl Peptidase Iv3.4.14.50100.0728 &Y*S%Y&D*H
2qjrA, 2qjrB, 3f8sA, 3f8sBDipepdyl Peptidase Iv In Complex With In3.4.14.50100.0728 &Y*S%Y&D*H
3noxA, 3noxB, 3swwA, 3swwB, 3sx4A, 3sx4B, 3q0tA, 3q0tBHuman Dpp-Iv In Complex With Sa-(+)-(6- 3.4.14.50100.0728 &Y*S%Y&D*H
1x70A, 1x70B, 2fjpA, 2fjpB, 2hhaA, 2hhaB, 2iitA, 2iitB, 2iivA, 2iivB, 2ophA, 2ophB, 2p8sA, 2p8sB, 2qoeA, 2qoeB, 3c43A, 3c43B, 3c45A, 3c45B, 3d4lA, 3d4lB, 2qkyA, 2qkyB, 2qkyC, 2qkyD, 3habA, 3habB, 3hacA, 3hacBHuman Dipeptidyl Peptidase Iv In Complex3.4.14.5099.9728 &Y*S%Y&D*H
2qt9A, 2qt9B, 2qtbA, 2qtbBHuman Dipeptidyl Peptidase IvCD26 IN COM3.4.14.5099.9728 &Y*S%Y&D*H
1u8eA, 1u8eBHuman Dipeptidyl Peptidase IvCD26 MUTANT3.4.14.5099.9728 &F*S%Y&D*H
4a5sA, 4a5sBHuman Dpp4 In Complex With A Noval Heter099.9728 &Y*S%Y&D*H
2oncA, 2oncB, 2oncC, 2oncDHuman Dpp-43.4.14.5099.9728 &Y*S%Y&D*H
2g5pA, 2g5pB, 2g5tA, 2g5tB, 2g63A, 2g63B, 2g63C, 2g63D, 2i03A, 2i03B, 2i03C, 2i03D, 2oqvA, 2oqvB, 2i78A, 2i78B, 2i78C, 2i78D, 2oagA, 2oagB, 2oagC, 2oagDHuman Dipeptidyl Peptidase Iv (Dppiv) Co3.4.14.50100.0726 &Y*S%Y&D*H
3q8wA, 3q8wBA B-Aminoacyl Containing Thiazolidine De3.4.14.50100.0726 &Y*S%Y&D*H
3qbjA, 3qbjBDipeptidyl Peptidase Iv In Complex With 099.7728 &Y*S%Y&D*H
1orvA, 1orvB, 1orvC, 1orvD, 1orwA, 1orwB, 1orwC, 1orwD, 2buaA, 2buaB, 2buaC, 2buaD, 2bucA, 2bucB, 2bucC, 2bucD, 2aj8A, 2aj8B, 2aj8C, 2aj8D, 2ajbA, 2ajbB, 2ajbC, 2ajbD, 2ajcA, 2ajcB, 2ajcC, 2ajcD, 2ajdA, 2ajdB, 2ajdC, 2ajdDPorcine Dipeptidyl Peptidase Iv (Cd26)3.4.14.5088.2728 &Y*S%Y&D*H
2gbcA, 2gbcB, 2gbfA, 2gbfB, 2gbgA, 2gbgB, 2gbiA, 2gbiB, 2i3zA, 2i3zB, 2oaeA, 2oaeB, 4ffvA, 4ffvB, 4ffwA, 4ffwBNative Dpp-Iv (Cd26) From Rat3.4.14.5084.6729 &Y*S%Y&D*H
1z68A, 1z68BHuman Fibroblast Activation Protein Alph5.7e-17953.2726 &Y*S%Y&D*H
1xfdA, 1xfdB, 1xfdC, 1xfdDA Human A-Type Potassium Channel Acceler3.4e-9233.1746 &D*D%Y&D*H
2ecfADipeptidyl Aminopeptidase Iv From Stenot9.5e-4328.8683 &Y*S%N&D*H
2d5lA, 2eepAProlyl Tripeptidyl Aminopeptidase From P3.4.14.125.1e-3825.8730 &Y*S%Y&D*H
2dcmAThe S603a Mutated Prolyl Tripeptidyl Ami3.4.14.129.5e-3825.6730 &Y*A%Y&D*H
2z3wA, 2z3zAProlyl Tripeptidyl Aminopeptidase Mutant3.4.14.129.5e-3825.8730 &Y*S%Y&D*H
3azoA, 3azoBPuromycin Hydrolase1.3e-0726.5226 &H*S%A&D*H
3azpA, 3azpB, 3azqA, 3azqBPuromycin Hydrolase S511a Mutant3.9e-0726.1226 &H*A%A&D*H
2qzpA, 2qzpBMutation Of An Acylptide HydrolaseESTERA3.4.19.11.3e-0526.2210 &H*S%Y&D*H
1ve6A, 1ve6B, 1ve7A, 1ve7B, 2hu5A, 2hu5B, 2hu7A, 2hu7B, 3o4gA, 3o4gB, 3o4gC, 3o4gDAn Acylpeptide Hydrolase/esterase From A3.4.19.11.3e-0526.2210 &H*S%Y&D*H
2qr5A, 2qr5BAeropyrum Pernix Acylaminoacyl Peptidase3.4.19.12.5e-0526.2210 &A*S%Y&D*H
2hu8A, 2hu8BBinding Of Inhibitors By Acylaminoacyl P3.4.19.12.5e-0525.7210 &H*A%Y&D*H
3o4jA, 3o4jB, 3o4jC, 3o4jDStructure And Catalysis Of Acylaminoacyl3.4.19.13.3e-0525.7210 &H*S%Y&N*H
3o4hA, 3o4hB, 3o4hC, 3o4hD, 3o4iA, 3o4iBStructure And Catalysis Of Acylaminoacyl3.4.19.16.2e-0525.7210 &H*S%Y&A*H

Proteins identified as mutant are highlighted in maroon. Conservative changes in active site residues, e.g. &K, are marked in green. Non-conservative changes to active site residues (&A) are highlighted in red. Library sequence residues identical to MACie active site residues are shown in grey.

Likewise, E.C. numbers identical to the MACiE protein are shown in grey; differences in black.


Homologs in PDB for MACiE ID:


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