4O8H

0.85A resolution structure of PEG 400 Bound Cyclophilin D

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	7
Details	BINDING SITE FOR RESIDUE PEG A 201

Chain	Residue
A	ARG55
A	GLN63
A	ALA101
A	PHE113
A	HOH317
A	HOH511
A	HOH538

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE 1PE A 202

Chain	Residue
A	PRO95
A	HIS131
A	HOH411
A	HOH552
A	VAL93
A	GLY94

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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	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
A	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
A	LYS44
A	ILE133
A	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
A	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
A	CYS161

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