7TGV

Structure of Cyclophilin D Peptidyl-Prolyl Isomerase Domain bound to Macrocyclic Inhibitor B2

Functional Information from GO Data

Chain	GOid	namespace	contents
X	0000413	biological_process	protein peptidyl-prolyl isomerization
X	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
X	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
X	TYR48-GLY65

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KR7

Chain	Residue	Details
X	LYS25

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site_id	SWS_FT_FI2
Number of Residues	3
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q99KR7

Chain	Residue	Details
X	LYS44
X	ILE133
X	LYS148

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q99KR7

Chain	Residue	Details
X	LYS125

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:Q99KR7

Chain	Residue	Details
X	CYS161

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