3ICI

Crystal structure of cyclophilin B in complex with calmegin fragment

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000413	biological_process	protein peptidyl-prolyl isomerization
A	0003723	molecular_function	RNA binding
A	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
A	0005515	molecular_function	protein binding
A	0005518	molecular_function	collagen binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005783	cellular_component	endoplasmic reticulum
A	0005788	cellular_component	endoplasmic reticulum lumen
A	0005790	cellular_component	smooth endoplasmic reticulum
A	0005829	cellular_component	cytosol
A	0005925	cellular_component	focal adhesion
A	0006457	biological_process	protein folding
A	0016018	molecular_function	cyclosporin A binding
A	0016020	cellular_component	membrane
A	0016853	molecular_function	isomerase activity
A	0030593	biological_process	neutrophil chemotaxis
A	0032991	cellular_component	protein-containing complex
A	0034663	cellular_component	endoplasmic reticulum chaperone complex
A	0040018	biological_process	positive regulation of multicellular organism growth
A	0042470	cellular_component	melanosome
A	0044794	biological_process	host-mediated activation of viral process
A	0044829	biological_process	host-mediated activation of viral genome replication
A	0048471	cellular_component	perinuclear region of cytoplasm
A	0050821	biological_process	protein stabilization
A	0051082	molecular_function	unfolded protein binding
A	0060348	biological_process	bone development
A	0070062	cellular_component	extracellular exosome
A	0070063	molecular_function	RNA polymerase binding
A	1901873	biological_process	regulation of post-translational protein modification
B	0000413	biological_process	protein peptidyl-prolyl isomerization
B	0003723	molecular_function	RNA binding
B	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
B	0005515	molecular_function	protein binding
B	0005518	molecular_function	collagen binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005783	cellular_component	endoplasmic reticulum
B	0005788	cellular_component	endoplasmic reticulum lumen
B	0005790	cellular_component	smooth endoplasmic reticulum
B	0005829	cellular_component	cytosol
B	0005925	cellular_component	focal adhesion
B	0006457	biological_process	protein folding
B	0016018	molecular_function	cyclosporin A binding
B	0016020	cellular_component	membrane
B	0016853	molecular_function	isomerase activity
B	0030593	biological_process	neutrophil chemotaxis
B	0032991	cellular_component	protein-containing complex
B	0034663	cellular_component	endoplasmic reticulum chaperone complex
B	0040018	biological_process	positive regulation of multicellular organism growth
B	0042470	cellular_component	melanosome
B	0044794	biological_process	host-mediated activation of viral process
B	0044829	biological_process	host-mediated activation of viral genome replication
B	0048471	cellular_component	perinuclear region of cytoplasm
B	0050821	biological_process	protein stabilization
B	0051082	molecular_function	unfolded protein binding
B	0060348	biological_process	bone development
B	0070062	cellular_component	extracellular exosome
B	0070063	molecular_function	RNA polymerase binding
B	1901873	biological_process	regulation of post-translational protein modification
C	0005509	molecular_function	calcium ion binding
C	0005783	cellular_component	endoplasmic reticulum
C	0006457	biological_process	protein folding
C	0051082	molecular_function	unfolded protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 401

Chain	Residue
A	GLY-3
A	ASP2
B	HIS134
B	HOH928

---

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE MES A 402

Chain	Residue
B	LYS172
B	GLU174
B	HOH623
B	HOH812
B	HOH822
A	LYS84
A	GLY88
A	GLU89
B	THR49
B	GLY171

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 401

Chain	Residue
A	HIS134
B	GLY-3
B	ASP2
B	HOH501

---

Functional Information from PROSITE/UniProt

site_id	PS00170
Number of Residues	18
Details	CSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YknSkFHRVIkdFMiQGG

Chain	Residue	Details
A	TYR56-GLY73

---

site_id	PS00805
Number of Residues	13
Details	CALRETICULIN_REPEAT Calreticulin family repeated motif signature. IpDpNaeKPDDWN

Chain	Residue	Details
C	ILE322-ASN334

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	314
Details	Domain: {"description":"PPIase cyclophilin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00156","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	Motif: {"description":"Prevents secretion from ER"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q99KR7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q99KR7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"UniProtKB","id":"Q99KR7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P24369","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---