Structure for peptidase S01.191: complement factor D

Summary Gene structure Alignment Tree Sequences Sequence features Distribution Structure Literature Substrates

PDB	Organism	Resolution	Comment
1BIO	Homo sapiens	1.50 Å	complex with isatoic anhydride inhibitor
Catalytic residues are shown in ball-and-stick representation: His66 in purple, Asp114 in pink and Ser208 in orange.

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TERTIARY STRUCTURE DATA
Comment	Resolution	PDB	PDBe	SCOP	CATH	PDBSum	Proteopedia	Reference
Homo sapiens
complex with isatoic anhydride inhibitor	1.50 Å	1BIO	1BIO	1BIO	1BIO	1BIO	1BIO	Jing et al., 1998
complex with di-isopropyl fluorophosphate	2.40 Å	1DFP	1DFP	1DFP	1DFP	1DFP	1DFP	Cole et al., 1997
complex with 3,4-dichloroisocoumarin	1.80 Å	1DIC	1DIC	1DIC	1DIC	1DIC	1DIC	Cole et al., 1998
mutant with enhanced catalytic activity	2.00 Å	1DST	1DST	1DST	1DST	1DST	1DST	Kim et al., 1995
mature peptidase	2.00 Å	1DSU	1DSU	1DSU	1DSU	1DSU	1DSU	Narayana et al., 1994
precursor	2.10 Å	1FDP	1FDP	1FDP	1FDP	1FDP	1FDP	Jing et al., 1999
P21 crystal form	2.30 Å	1HFD	1HFD	1HFD	1HFD	1HFD	1HFD	Jing et al., 1998
mature peptidase	1.20 Å	2XW9	2XW9	2XW9	2XW9	2XW9	2XW9	Forneris et al., 2010
mature peptidase	2.80 Å	2XWA	2XWA	2XWA	2XWA	2XWA	2XWA	Forneris et al., 2010
mature peptidase	3.49 Å	2XWB	2XWB	2XWB	2XWB	2XWB	2XWB	Forneris et al., 2010
mature peptidase	1.80 Å	4CBN	4CBN	4CBN	4CBN	4CBN	4CBN	Forneris et al., 2014
mature peptidase	1.80 Å	4CBO	4CBO	4CBO	4CBO	4CBO	4CBO	Forneris et al., 2014
mature peptidase	2.42 Å	4D9R	4D9R	4D9R	4D9R	4D9R	4D9R	Katschke et al., 2012
complex with compound2	1.43 Å	5FBE	5FBE	5FBE	5FBE	5FBE	5FBE
complex with compound 3b	1.47 Å	5FBI	5FBI	5FBI	5FBI	5FBI	5FBI
complex with compound 5	1.86 Å	5FCK	5FCK	5FCK	5FCK	5FCK	5FCK
complex with a reversible indole carboxylic acid based inhibitor	1.29 Å	5MT0	5MT0	5MT0	5MT0	5MT0	5MT0
complex with a reversible benzoic acid based inhibitor	1.65 Å	5MT4	5MT4	5MT4	5MT4	5MT4	5MT4
complex with the inhibitor (s)-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1h-indol-3-yl)-amide] 2-[(3- trifluoromethoxy-phenyl)-amide]	1.55 Å	5NAR	5NAR	5NAR	5NAR	5NAR	5NAR
complex with the inhibitor (s)-pyrrolidine-1,2-dicarboxylic acid 1-[(1-methyl-1h-indol-3-yl)-amide] 2-[(3- trifluoromethoxy-phenyl)-amide]	1.17 Å	5NAT	5NAT	5NAT	5NAT	5NAT	5NAT
complex with the inhibitor (1r,3s,5r)-2-aza- bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1h-indol- 3-yl)-amide] 3-[(3-trifluoromethoxy-phenyl)-amide]	1.25 Å	5NAW	5NAW	5NAW	5NAW	5NAW	5NAW
complex with the inhibitor (2s,4s)-4-amino- pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1h-indol-3-yl)- amide] 2-[(3-trifluoromethoxy-phenyl)-amide]	1.75 Å	5NB6	5NB6	5NB6	5NB6	5NB6	5NB6
complement factor d	1.33 Å	5NB7	5NB7	5NB7	5NB7	5NB7	5NB7
complex with the inhibitor (2s,4r)-4-fluoro- pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1h-indol-3-yl)- amide] 2-[(3-trifluoromethoxy-phenyl)-amide]	1.87 Å	5NBA	5NBA	5NBA	5NBA	5NBA	5NBA
complement factor d inhibited with jh3	3.15 Å	5TCA	5TCA	5TCA	5TCA	5TCA	5TCA
complement factor d inhibited with jh4	3.37 Å	5TCC	5TCC	5TCC	5TCC	5TCC	5TCC
complex with compound 5	1.67 Å	6FTY	6FTY	6FTY	6FTY	6FTY	6FTY
complex with compound 6	1.67 Å	6FTZ	6FTZ	6FTZ	6FTZ	6FTZ	6FTZ
complex with the inhibitor 3-((3-((3- (aminomethyl)phenyl)amino)-1h-pyrazolo[3,4-d]pyrimidin-4-yl)amino) phenol	2.21 Å	6FUG	6FUG	6FUG	6FUG	6FUG	6FUG
complex with the inhibitor (4-((3- (aminomethyl)phenyl)amino)quinazolin-2-yl)-l-valine	1.37 Å	6FUH	6FUH	6FUH	6FUH	6FUH	6FUH
complex with the inhibitor 3-((3-((3- (aminomethyl)phenyl)amino)-1h-pyrazolo[3,4-d]pyrimidin-4-yl)amino) phenol	1.38 Å	6FUI	6FUI	6FUI	6FUI	6FUI	6FUI
Macaca mulatta
inhibiting alternative pathway complement activation by targeting the exosite on factor d	2.28 Å	4D9Q	4D9Q	4D9Q	4D9Q	4D9Q	4D9Q
Mus musculus
mouse complement factor d	1.25 Å	5FCR	5FCR	5FCR	5FCR	5FCR	5FCR