6R8L

Human Cyclophilin D in complex with 1-((1S,9S,10S)-10-Hydroxy-12-oxa-8-aza-tricyclo[7.3.1.02,7]trideca-2,4,6-trien-4-ylmethyl)-3- {2-[(R)-2-(2-methylsulfanyl-phenyl)-pyrrolidin-1-yl]-2-oxo-ethyl}-urea

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 PDB Data

site_id	AC1
Number of Residues	21
Details	binding site for residue JUZ A 301

Chain	Residue
A	ARG97
A	SER123
A	ALA143
A	ASN144
A	THR149
A	GLY151
A	GLN153
A	PHE155
A	LEU164
A	HIS168
A	SER191
A	ARG97
A	HOH449
A	HOH488
A	PHE102
A	MET103
A	GLN105
A	GLY114
A	THR115
A	GLY116
A	GLY117

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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	TYR90-GLY107

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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
A	LYS67

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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
A	LYS86
A	ILE175
A	LYS190

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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
A	LYS167

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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
A	CYS203

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