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Proteins in PDB homologous to 1btlA

109 proteins (330 PDB structures) with E() < 0.001

Homologs in SwissProt


Acc   E.C. E() % id alen 70
*S
73
*K
130
*S
166
*E
237
%A
1bt5A, 1jtgA, 1jtgC, 1axbA, 1btlA, 1temA, 3c7uA, 3c7uC, 3c7vA, 3c7vCThe Imipenem Inhibited Tem-1 Beta-Lactam3.5.2.63.6e-12099.2265 *S*K*S*E%A
1zg4ATem1 Beta Lactamase3.5.2.64e-12099.2265 *S*K*S*E%A
1jtdABeta-Lactamase Inhibitor Protein-Ii In C3.5.2.64.3e-12098.9265 *S*K*S*E%A
1ck3AN276d Mutant Of Escherichia Coli Tem-1 B3.5.2.68.5e-12098.9265 *S*K*S*E%A
1zg6ATem1 Beta Lactamase Mutant S70g3.5.2.69.5e-12098.9265 *G*K*S*E%A
1eroA, 1erqA, 1s0wA, 1s0wB, 1xpbA, 4gkuAX-Ray Tem-1 Beta Lactamase In Complex Wi3.5.2.61e-11998.5265 *S*K*S*E%A
1esuAS235a Mutant Of Tem1 Beta-Lactamase3.5.2.62e-11998.1265 *S*K*S*E%A
1yt4ATem-76 Beta-Lactamase At 1.4 Angstrom Re3.5.2.62.4e-11998.1265 *S*K*G*E%A
1li9ATem-34 Beta-lactamase At 1.5 Angstrom3.5.2.62.9e-11998.1265 *S*K*S*E%A
1fqgAMolecular The Acyl-Enzyme Intermediate I3.5.2.62.9e-11998.1265 *S*K*S*N%A
3jyiA, 3jyiB, 3jyiC, 3jyiD, 3jyiE, 3jyiFStructural And Biochemical Evidence That3.5.2.63.4e-11998.1265 *S*K*S*E%A
1jwvAG238a Mutant Of Tem-1 Beta-Lactamase In 3.5.2.64e-11998.1265 *S*K*S*E%A
1jwpA, 1m40A, 1nxyA, 1ny0A, 1nymA, 1nyyA, 1pzoAM182t Mutant Of Tem-1 Beta-Lactamase3.5.2.64e-11998.1265 *S*K*S*E%A
1lhyATem-30 Beta-lactamase At 2.0 Angstrom3.5.2.64e-11998.1265 *S*K*S*E%A
1jvjAN132a Mutant Of Tem-1 Beta-Lactamase In 3.5.2.64e-11998.1265 *S*K*S*E%A
1pzpATem-1 Beta-Lactamase In Complex With A N3.5.2.64e-11998.1265 *S*K*S*E%A
3cmzATem-1 Class-A Beta-Lactamase L201p Mutan3.5.2.64.8e-11998.1265 *S*K*S*E%A
1ermAX-Ray Tem-1 Beta Lactamase In Complex Wi3.5.2.64.8e-11998.1265 *S*K*S*E%A
1li0ATem-32 Beta-Lactamase At 1.6 Angstrom3.5.2.69.6e-11997.7265 *S*K*S*E%A
3gmwA, 3gmwCBeta-Lactamse Inhibitory Protein-I (Blip1.3e-11898.9263 *S*K*S*E%A
1xxmA, 1xxmBThe Modular Architecture Of Protein-Prot3.5.2.61.6e-11898.1265 *S*K*S*E%A
2b5rA, 2b5rB1b Lactamase B LACTAMASE INHIBITOR3.5.2.61.9e-11898.1265 *S*K*S*E%A
1htzA, 1htzB, 1htzC, 1htzD, 1htzE, 1htzFTem52 Beta-Lactamase3.8e-11897.4265 *S*K*S*E%A
1jwzATem-64 Beta-Lactamase In Complex With A 3.5.2.63.8e-11897.4265 *S*K*S*E%A
3p98A, 3p98BThe The Extended Spectrum Beta-Lactamase1e-11797.0265 *S*K*S*E%A
3dtmAIncreased Folding Stability Of Tem-1 Bet7e-11695.8265 *S*K*S*E%A
2v1zA, 2v20AA Tem-1 Beta-Lactamase Insertant Alloste3.5.2.61e-11394.1270 *S*K*S*E%A
3toiA, 3toiBTailoring Enzyme Stability And Exploitin2.5e-10796.0247 *S*K*S*E%A
4dxbA, 4dxbB, 4dxcA2.29a The Engineered Mbp Tem-1 Fusion Pr7.8e-9284.9252 *S*K*S*E%A
3n4iAThe Shv-1 D104e Beta-LactamaseBETA-Lacta3.5.2.63.1e-8267.8264 *S*K*S*E%A
1shvA, 1ongA, 1q2pA, 1vm1A, 2g2uA, 2h5sA, 3c4oA, 3c4pA, 2zd8A, 3mkeA, 3mkfA, 3mxrA, 3mxsA, 4fh4AShv-1 Beta-Lactamase3.5.2.66.2e-8267.4264 *S*K*S*E%A
3d4fAShv-1 Beta-Lactamase Complex With Ln1-253.5.2.66.8e-8267.4264 *S*K*S*E%A
2g2wAThe Shv D104k Beta-lactamase/beta-lactam3.5.2.67.4e-8267.4264 *S*K*S*E%A
1tdgA, 1tdlA, 3v50AComplex Of S130g Shv-1 Beta-Lactamase Wi3.5.2.61.5e-8167.0264 *S*K*G*E%A
3v5mAM69v Mutant Of Shv Beta-Lactamase1.7e-8167.0264 *S*K*S*E%A
1rcjAE166a Mutant Of Shv-1 Beta-Lactamase Wit3.5.2.62.1e-8167.0264 *S*K*S*A%A
2a49AClavulanic Acid Bound To E166a Variant O3.5.2.62.1e-8167.0264 *S*K*S*A%A
2a3uASulbactam Bound To E166a Variant Of Shv-3.5.2.62.1e-8167.0264 *S*K*S*A%A
3oplA, 3oprAEsbl R164h Mutant Shv-1 Beta-Lactamase3.5.2.62.3e-8167.0264 *S*K*S*E%A
1n9bAUltrahigh Resolution A Class A Beta-lact3.5.2.62.5e-8167.0264 *S*K*S*E%A
3ophA, 3oppAEsbl R164s Mutant Of Shv-1 Beta-Lactamas3.5.2.62.7e-8167.0264 *S*K*S*E%A
2h0tA, 2h0yA, 2h10AThe M69v E166a Double Mutant Of Shv-1 B-3.5.2.65.9e-8166.7264 *S*K*S*A%A
1g6aAPse-4 Carbenicillinase, R234k Mutant3.5.2.65.5e-4445.3254 *S*K*S*E%A
1g68APse-4 Carbenicillinase, Wild Type3.5.2.69.2e-4444.9254 *S*K*S*E%A
3e2kA, 3e2kBThe Kpc-2 Beta-LactamaseBETA-Lactamase I3.5.2.62.3e-4141.6250 *S*K*S*E%T
4eqiA, 4eqiBSerratia Fonticola Carbapenemase Sfc-12.5e-4142.6242 *S*K*S*E%T
2ov5A, 2ov5B, 2ov5CThe Kpc-2 Carbapenemase2.7e-4141.6250 *S*K*S*E%T
3c5aA, 3rxwA, 3rxxAThe C-Terminal Deleted Mutant Of The Cla2.7e-4141.6250 *S*K*S*E%T
3dw0A, 3dw0BThe Class A Carbapenemase Kpc-2 At 1.6 A3.1e-4141.6250 *S*K*S*E%T
4euzASerratia Fonticola Carbapenemase Sfc-1 S5e-4142.1242 *A*K*S*E%T
3e2lA, 3e2lBThe Kpc-2 Beta-LactamaseBETA-Lactamase I3.5.2.66.4e-4141.2250 *X*K*S*E%T
3bydABeta-Lactamase Oxy-1-1 From Klebsiella O3.5.2.67.8e-4141.1258 *S*K*S*E%A
4ev4ASerratia Fonticola Carbapenemase Sfc-1 E8.4e-4142.1242 *S*K*S*A%T
1n4oA, 1n4oB, 1o7eA, 1o7eBThe Class A Beta-Lactamase L2 From Steno1.9e-4042.5247 *S*K*S*E%S
1iysAClass A Beta-Lactamase Toho-13.5.2.62.4e-3939.4254 *S*K*S*E%S
3bfeA, 3bfeB, 3bfeC, 3bfeDThe Class A Beta-Lactamase Sed-1 From Ci4.1e-3942.3239 *S*K*S*E%A
3b3xA, 3b3xB, 2wk0A, 2wk0B, 2x71A, 2x71B, 4a5rA, 4a5rBClass A Beta-Lactamase Of Bacillus Liche3.5.2.67e-3940.2254 *S*K*S*E%A
1iyoA, 1iypA, 1iyqA, 1bzaAToho-1 Beta-Lactamase In Complex With Ce3.5.2.68.1e-3939.0254 *S*K*S*A%S
1w7fA, 1w7fBThe Class A Beta-Lactamase Bs3 Inhibited8.4e-3940.2254 *S*K*S*E%A
1i2sA, 1i2sB, 1i2wA, 1i2wBBeta-Lactamase From Bacillus Licheniform3.5.2.61.1e-3840.2254 *S*K*S*E%A
1we4AClass A Beta-Lactamase Toho-1 G238c Muta3.5.2.61.4e-3839.0254 *S*K*S*E%S
2xr0ARoom Temperature The Perdeuterated Toho-3.5.2.61.6e-3839.0254 *S*K*S*E%S
2xqzANeutron The Perdeuterated Toho-1 R274n R3.5.2.61.6e-3839.0254 *S*K*S*E%S
2zq8AApo Class A Beta-Lactamase Toho-1 R274nR3.5.2.61.6e-3839.0254 *S*K*S*E%S
2y91A, 2y91BClass A Beta-Lactamase From Bacillus Lic2e-3839.8254 *X*K*S*E%A
3bfcA, 3bfcB, 3bfcC, 3bfcD, 3bffA, 3bffB, 3bffC, 3bffD, 3bfgA, 3bfgB, 3bfgC, 3bfgDClass A Beta-Lactamase Sed-G238c Complex2.3e-3841.8239 *S*K*S*E%A
3bfdA, 3bfdB, 3bfdC, 3bfdDThe Class A Beta-lactamase Sed-g238c Mut2.3e-3841.8239 *S*K*S*E%A
2zq7A, 2zq9A, 2zqaA, 2zqcA, 2zqdAApo Class A Beta-Lactamase Toho-1 E166aR3.5.2.65.5e-3838.6254 *S*K*S*A%S
2blmA, 2blmB, 4blmA, 4blmBBeta-Lactamase Of Bacillus Licheniformis3.5.2.61.1e-3739.4254 *S*K*S*E%A
2cc1AThe Class A Beta-Lactamase From Mycobact3.5.2.61.3e-3744.9227 *S*K*S*E%S
1yltA, 1ylzA, 1ylzBCtx-M-14 Beta-Lactamase1.3e-3739.3257 *S*K*S*E%S
3qhyAStructural, Thermodynamic And Kinetic An1.4e-3740.9252 *S*K*S*E%A
2wyxANeutron A Class A Beta-Lactamase Toho-13.5.2.61.8e-3739.2245 *S*K*S*A%S
1ylpACtx-M-27 Beta-Lactamase1.9e-3739.3257 *S*K*S*E%S
2p74A, 2p74B, 3g2yA, 3g2yB, 4ddsA, 4ddsB, 4ddyA, 4ddyB, 4de0A, 4de0B, 4de1A, 4de1B, 4de2A, 4de2B, 4de3A, 4de3BCtx-M-9 Class A Beta-Lactamase Apo Cryst3.1e-3739.3257 *S*K*S*E%S
1yljA, 1ylyA, 1ylyB, 1ym1A, 1ym1B, 1ymsA, 1ymsB, 1ymxA, 1ymxB, 3g2zA, 3g2zB, 3g30A, 3g31A, 3g31B, 3g32A, 3g32B, 3g34A, 3g34B, 3g35A, 3g35BCtx-M-9 Beta-Lactamase3.1e-3739.3257 *S*K*S*E%S
1mblA, 1mblBA Catalytically-Impaired Class A Beta-La3.5.2.63.6e-3739.0254 *S*K*S*A%A
3ly4A, 3m2jA, 3m2jB, 3m2kA, 3m2kBFluorophore-Labeled Class A -Lactamase P3.5.2.65.1e-3739.0254 *S*K*S*C%A
3ly3AFluorophore-Labeled Class A Beta-Lactama3.5.2.65.1e-3739.0254 *S*K*S*C%A
3sh7A, 3sh7B, 3sh8A, 3sh8B, 3sh9A, 3sh9BFluorophore-Labeled Beta-Lactamase Penp3.5.2.65.3e-3739.0254 *S*K*S*C%A
1ylwACtx-m-16 Beta-lactamase6.2e-3739.3257 *S*K*S*E%S
3huoA, 3huoB, 3hvfA, 3hvfB, 3hlwA, 3hlwB, 3hreA, 3hreB, 3q07A, 3q07B, 3q1fA, 3q1fBX-Ray Crystallographic Ctx-M-9 S70g In C7.4e-3738.9257 *G*K*S*E%S
1dy6A, 1dy6BThe Imipenem-Hydrolyzing Beta-Lactamase 2.5e-3635.9251 *S*K*S*E%S
3lezAA Halotolerant Bacterial Beta-Lactamase3.5e-3639.3247 *S*K*S*E%A
1bsgABeta-Lactamase From Streptomyces Albus G3.5.2.63.6e-3641.5241 *S*K*S*E%A
1hzoA, 1hzoBClass A Cephalosporinase From Proteus Vu3.5.2.65.2e-3640.4255 *S*K*S*E%S
3soiA, 3soiBCrystallographic Bacillus Licheniformis 1.6e-3538.6254 *S*K*S*E%A
1bueA, 1bulANmc-A Carbapenemase From Enterobacter Cl3.5.2.63.4e-3535.1251 *S*K*S*E%S
3ni9A, 3ni9B, 3niaAGes-2 Carbapenemase Apo Form6.9e-3538.7248 *S*K*S*E%T
2qpnA, 2qpnBGes-1 Beta-Lactamase2.5e-3438.3248 *S*K*S*E%T
3cg5A, 3dwzA, 3iqaA, 3m6bA, 3m6hA, 4df6AThe Covalent Adduct Formed Between Tb B-3.5.2.61.4e-3137.5256 *S*K*S*E%T
2gdnAThe Mycobacterium Tuberculosis Beta- Lac3.5.2.61.4e-3137.5256 *S*K*S*E%T
3n8sA, 3n6iA, 3n7wA, 3n8lA, 3n8rA, 3nblA, 3nc8A, 3nckA, 3ndeA, 3ndgA, 4eblA, 4eblB, 4eblC, 4eblD, 4ebnA, 4ebnB, 4ebnC, 4ebnD, 4ebpA, 4ebpB, 4ebpC, 4ebpDBlac-E166a Covalently Bound With Cefaman3.5.2.64.7e-3137.1256 *S*K*S*A%T
3ny4ABlac-K73a Bound With Cefamandole3.5.2.64.7e-3137.1256 *S*A*S*E%T
1blcA, 1blhA, 3blmAInhibition Of Beta-Lactamase By Clavulan3.5.2.63.9e-2831.3259 *S*K*S*E%Q
1omeA, 1omeBThe Omega Loop Deletion Mutant (Residues3.5.2.63.9e-2831.3259 *S*K*S*E%Q
1djbA, 1djcABeta-Lactamase Precursor, S70a Mutant, A3.5.2.67.7e-2830.9259 *A*K*S*E%Q
1blpAStructural Basis For The Inactivation Of3.5.2.61.1e-2730.9259 *S*K*S*E%Q
1djaABeta-Lactamase Precursor, K73h Mutant, A3.5.2.61.1e-2730.9259 *S*H*S*E%Q
1kgfABeta-Lactamase Asn 170 Gln Mutant3.5.2.61.3e-2730.9259 *S*K*S*E%Q
1kggABeta-Lactamase Glu166gln:asn170asp Mutan3.5.2.61.9e-2730.5259 *S*K*S*Q%Q
1kgeABeta-Lactamase Asn 170 Met Mutant3.5.2.61.9e-2730.9259 *S*K*S*E%Q
1pioA, 1pioBAn Engineered Staphylococcus Aureus Pc1 3.5.2.62.2e-2731.3259 *S*K*S*E%Q
1ghiA, 1ghmA, 1ghpABeta-Lactamase Glu166asp:asn170gln Mutan3.5.2.62.6e-2730.5259 *S*K*S*D%Q
1alqACircularly Permuted Beta-Lactamase From 3.5.2.61.5e-2533.5221 *S*K*S*E%Q
3p09A, 3p09BBeta-Lactamase From Francisella Tularens1.3e-2126.6263 *S*K*S*E%T
1e25AThe High Resolution Per-1 Class A Beta- 3.5.2.61.2e-1326.5234 *S*K*S*E%A
2j9oA, 2j9oB, 2j9oC, 2j9oD, 2jbfA, 2jbfB, 2jbfC, 2jbfDPbp-A, L158e Mutant8e-1129.1230 *S*K*S*E%I
2j7vA, 2j7vB, 2j7vC, 2j7vD, 2j8yA, 2j8yB, 2j8yC, 2j8yDPbp-A3.8e-1028.7230 *S*K*S*L%I

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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