Proteins in PDB homologous to 2frvB

21 proteins (70 PDB structures) with E() < 0.001

Homologs in SwissProt

Acc   E.C. E() % id alen 18
2frvL, 2frvB, 2frvD, 2frvF, 2frvH, 2frvJThe Oxidized Form Of Ni-Fe Hydrogenase1.12.2.10100.0530 *E&C&C&H&R&S*C&C
1yq9H, 1yq9IThe Unready Oxidized Form Of [nife] Hydr1.12.2.1099.6530 *E&C&C&H&R&S*C&C
1frvB, 1frvDThe Oxidized Form Of Ni-Fe Hydrogenase1.12.2.1099.2530 *E&C&C&H&R&S*C&C
1ubhL, 1ubjL, 1ubkL, 1ublL, 1ubmL, 1uboL, 1ubrL, 1ubtL, 1ubuLThree-Dimensional The Carbon Monoxide Co1. *E&C&C&H&R&S*C&C
1h2rLThree-Dimensional Ni-Fe Hydrogenase From1. *E&C&C&H&R&S*C&C
1h2aLSingle Crystals Of Hydrogenase From Desu1. *E&C&C&H&R&S*C&C
1wujL, 1wukL, 1wulLThree-Dimensional The Ni-B State Of [nif1. *E&C&C&H&R&S*X&C
1wuhL, 1wuiLThree-Dimensional The Ni-A State Of [nif1. *E&C&X&H&R&S*X&C
3h3xQ, 3h3xR, 3h3xSThe V74m Large Subunit Mutant Of Ni-Fe H1. *E&C&C&H&R&S*C&C
3curH, 3curI, 3curJA Double Methionine Mutant Of Ni-Fe Hydr1. *E&C&C&H&R&S*C&C
1yrqH, 1yrqI, 1yrqJ, 1yrqK, 1yrqM, 1yrqNThe Ready Oxidized Form Of [nife]-Hydrog1.12.2.11e-15665.6535 *E&C&C&H&R&S*C&C
1yqwQ, 1yqwR, 1yqwSThe Oxidized Unready Form Of Ni-Fe Hydro1.12.2.12e-15665.4535 *E&C&C&H&R&A*C&C
3cusQ, 3cusR, 3cusSA Double IlePHE MUTANT OF NI-Fe Hydrogen1. *E&C&C&H&R&S*X&C
1frfLThe Ni-Fe Hydrogenase From Desulfovibrio1. *E&C&C&H&R&S*C&C
1e3dB, 1e3dD[nife] Hydrogenase From Desulfovibrio De1.6e-15162.7531 *E&C&C&H&R&T*C&C
3myrB, 3myrD, 3myrF, 3myrH[nife] Hydrogenase From Allochromatium V6.2e-11449.2561 *E&C&C&H&R&S*C&C
3uqyL, 3uqyM, 3uscL, 3uscM, 3useL, 3useM, 4gd3L, 4gd3M, 4gd3J, 4gd3KH2-Reduced E. Coli Hydrogenase-11.8e-9943.2569 *E&C&C&H&R&T*C&C
3ayxA, 3ayxC, 3ayyA, 3ayyC, 3ayzA, 3ayzCMembrane-Bound Respiratory [nife] Hydrog1.3e-9642.5583 *E&C&C&H&R&T*C&C
3rgwLCrystal Structure At 1.5 A Resolution Of1.12.99.63e-9442.0593 *E&C&C&H&R&T*C&C
2wpnBThe Oxidised, As-Isolated Nifese Hydroge6e-6336.1537 *E&X&C&H&R&S*X&C
1cc1LA Reduced, Active Form Of The Ni-Fe-Se H1. *E&C&C&H&R&T*X&C

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:

Contact Us Glossary of Terms Useful Links Statistics Documentation More about MACiE