8EJX

Crystal structure of human cyclophilin D (CypD) with in complex with the covalently bound Ebselen inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000413	biological_process	protein peptidyl-prolyl isomerization
A	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
A	0006457	biological_process	protein folding

Functional Information from PROSITE/UniProt

site_id	PS00170
Number of Residues	18
Details	CSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YkgStFHRVIpsFMcQAG

Chain	Residue	Details
A	TYR48-GLY65

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q99KR7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	3
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q99KR7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q99KR7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"UniProtKB","id":"Q99KR7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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