Structure for peptidase S33.005: tricorn interacting factor F1

Summary Alignment Tree Sequences Sequence features Distribution Structure Literature Substrates

PDB	Organism	Resolution	Comment
1MTZ	Thermoplasma acidophilum	1.80 Å	mature
Catalytic residues are shown in ball-and-stick representation: Ser105 in orange, Asp244 in pink and His271 in purple.

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TERTIARY STRUCTURE DATA
Comment	Resolution	PDB	PDBe	SCOP	CATH	PDBSum	Proteopedia	Reference
Thermoplasma acidophilum
Methionine residues modified to selenomethionine.	2.00 Å	1MT3	1MT3	1MT3	1MT3	1MT3	1MT3	Goettig et al., 2002
mature peptidase	1.80 Å	1MTZ	1MTZ	1MTZ	1MTZ	1MTZ	1MTZ	Goettig et al., 2002
complex with 3-amino-1-chloro-4-phenyl-butanol-2-yl.	2.40 Å	1MU0	1MU0	1MU0	1MU0	1MU0	1MU0	Goettig et al., 2002
inactive F1-mutant Gly37Ala	2.30 Å	1XQV	1XQV	1XQV	1XQV	1XQV	1XQV	Goettig et al., 2005
F1-mutant Ser105Ala complex with Phe-Leu	2.00 Å	1XQW	1XQW	1XQW	1XQW	1XQW	1XQW	Goettig et al., 2005
F1-mutant Ser105Ala; complex with PCK	2.10 Å	1XQX	1XQX	1XQX	1XQX	1XQX	1XQX	Goettig et al., 2005
Ser105Ala mutant; complex with Pro-Leu-Gly-Gly	3.20 Å	1XQY	1XQY	1XQY	1XQY	1XQY	1XQY	Goettig et al., 2005
active site F1-mutant Tyr205Phe complex with inhibitor PCK	1.82 Å	1XRL	1XRL	1XRL	1XRL	1XRL	1XRL	Goettig et al., 2005
active site F1-mutant Glu213Gln soaked with peptide Ala-Phe	2.70 Å	1XRM	1XRM	1XRM	1XRM	1XRM	1XRM	Goettig et al., 2005
active site F1-mutant Glu213Gln soaked with peptide Phe-Ala	2.80 Å	1XRN	1XRN	1XRN	1XRN	1XRN	1XRN	Goettig et al., 2005
active site F1-mutant Glu213Gln soaked with peptide Phe-Leu	1.80 Å	1XRO	1XRO	1XRO	1XRO	1XRO	1XRO	Goettig et al., 2005
active site F1-mutant Glu213Gln soaked with peptide Pro-Leu-Gly-Gly	2.30 Å	1XRP	1XRP	1XRP	1XRP	1XRP	1XRP	Goettig et al., 2005
active site F1-mutant Glu245Gln soaked with peptide Phe-Leu	2.80 Å	1XRQ	1XRQ	1XRQ	1XRQ	1XRQ	1XRQ	Goettig et al., 2005
active site F1-mutant Glu245Gln soaked with peptide Pro-Pro	2.40 Å	1XRR	1XRR	1XRR	1XRR	1XRR	1XRR	Goettig et al., 2005