Proteins in PDB homologous to 1chmA

25 proteins (82 PDB structures) with E() < 0.001

Homologs in SwissProt

Acc   E.C. E() % id alen 232
1chmBEnzymatic Mechanism Of Creatine Amidinoh3. *H&E&E
1chmAEnzymatic Mechanism Of Creatine Amidinoh3. *H&E&E
1kp0A, 1kp0BThe Crystal Structure Analysis Of Creati9e-11763.2400 *H&E&E
3q6dA, 3q6dB, 3q6dC, 3q6dDXaa-Pro Dipeptidase From Bacillus Anthra7.2e-1825.4370 *H&T&E
1wn1A, 1wn1B, 2howA, 2howBDipeptiase From Pyrococcus Horikoshii Ot9e-1424.2372 *H&T&E
1wy2A, 1wy2BThe Prolidase From Pyrococcus Horikoshii3. *H&T&E
1pv9A, 1pv9BProlidase From Pyrococcus Furiosus3. *H&T&E
2zsgA, 2zsgBX-Pro Aminopeptidase From Thermotoga Mar1.3e-1021.6380 *H&T&E
4egeADipeptidase Pepe From Mycobacterium Ulce9.1e-0924.5384 *H&T&E
2bwuAAsp271ala Escherichia Coli Aminopeptidas3. *H&T&E
1wl9A, 1w2mA, 1w2mB, 1w2mC, 1w2mD, 1w2mE, 1w2mF, 1w7vA, 1w7vB, 1w7vC, 1w7vD, 1wbqA, 1wbqB, 1wbqC, 1wbqDAminopeptidase P From E. Coli3. *H&T&E
2bwwAHis350ala Escherichia Coli Aminopeptidas3. *H&T&E
2bwvA, 2v3yAHis361ala Escherichia Coli Aminopeptidas3. *H&T&E
1jawAAminopeptidase P From E. Coli Low Ph For3. *H&T&E
1m35A, 1m35B, 1m35C, 1m35D, 1m35E, 1m35F, 1n51A, 1wl6A, 1wlrA, 2bhaA, 2bhbA, 2bhcA, 2bhdA, 1a16A, 2bh3A, 2bn7AAminopeptidase P From Escherichia Coli3. *H&T&E
2bwtAAsp260ala Escherichia Coli Aminopeptidas3. *H&T&E
2v3zAGlu383ala Escherichia Coli Aminopeptidas3. *H&T&A
2bwyAGlu383ala Escherichia Coli Aminopeptidas3.4.11.98e-0624.5290 *H&T&A
4fukA, 4fukBAminopeptidase From Trypanosoma Brucei9.1e-0625.7140 *H&N&E
3mr1A, 3mr1B, 3mr1C, 3mr1DMethionine Aminopeptidase From Ricketts *H&S&E
3mx6A, 3mx6BMethionine Aminopeptidase From Ricketts *H&S&E
2bwsA, 2v3xAHis243ala Escherichia Coli Aminopeptidas3. *A&T&E
1o0xAMethionine Aminopeptidase (Tm1478) From 1.8e-0528.3191 *H&A&E
2bwxAHis354ala Escherichia Coli Aminopeptidas3.4.11.96e-0523.6288 *H&T&E
1qxwA, 1qxyA, 1qxzAStaphyloccocus Aureus In Complex With An3. *H&T&E

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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