4J5C

Human Cyclophilin D Complexed with an Inhibitor

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 PDB Data

site_id	AC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE 7I6 X 301

Chain	Residue
X	ARG97
X	GLN153
X	PHE155
X	LEU164
X	HIS168
X	HOH471
X	HOH484
X	HOH494
X	HOH507
X	HOH567
X	HOH615
X	MET103
X	HOH640
X	HOH746
X	GLN105
X	GLY114
X	ARG124
X	ALA143
X	ASN144
X	THR149
X	GLY151

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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
X	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
X	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
X	LYS86
X	ILE175
X	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
X	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
X	CYS203

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