3RD9

Human Cyclophilin D Complexed with a Fragment

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	26
Details	BINDING SITE FOR RESIDUE MSY X 301

Chain	Residue
X	HIS96
X	GLN153
X	HIS168
X	HOH461
X	HOH509
X	HOH695
X	HOH696
X	HOH697
X	HOH700
X	HOH704
X	HOH709
X	ARG97
X	HOH710
X	HOH711
X	HOH713
X	HOH714
X	HOH718
X	HOH757
X	HOH766
X	GLN105
X	ASN113
X	GLY114
X	PHE130
X	LYS133
X	ALA143
X	ASN144

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG X 302

Chain	Residue
X	PRO100
X	SER101
X	HOH708
X	HOH725
X	HOH726

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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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