Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2P6B

Crystal Structure of Human Calcineurin in Complex with PVIVIT Peptide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016787	molecular_function	hydrolase activity
A	0033192	molecular_function	calmodulin-dependent protein phosphatase activity
A	0097720	biological_process	calcineurin-mediated signaling
B	0004721	molecular_function	phosphoprotein phosphatase activity
B	0004723	molecular_function	calcium-dependent protein serine/threonine phosphatase activity
B	0005509	molecular_function	calcium ion binding
B	0005515	molecular_function	protein binding
B	0005516	molecular_function	calmodulin binding
B	0005654	cellular_component	nucleoplasm
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0005955	cellular_component	calcineurin complex
B	0008287	cellular_component	protein serine/threonine phosphatase complex
B	0008597	molecular_function	calcium-dependent protein serine/threonine phosphatase regulator activity
B	0019902	molecular_function	phosphatase binding
B	0019904	molecular_function	protein domain specific binding
B	0033173	biological_process	calcineurin-NFAT signaling cascade
B	0042383	cellular_component	sarcolemma
B	0045202	cellular_component	synapse
B	0045944	biological_process	positive regulation of transcription by RNA polymerase II
B	0046872	molecular_function	metal ion binding
B	0070886	biological_process	positive regulation of calcineurin-NFAT signaling cascade
B	0098685	cellular_component	Schaffer collateral - CA1 synapse
B	0098686	cellular_component	hippocampal mossy fiber to CA3 synapse
B	0098688	cellular_component	parallel fiber to Purkinje cell synapse
B	0098693	biological_process	regulation of synaptic vesicle cycle
B	0098794	cellular_component	postsynapse
B	0098978	cellular_component	glutamatergic synapse
B	0099149	biological_process	regulation of postsynaptic neurotransmitter receptor internalization
B	0099170	biological_process	postsynaptic modulation of chemical synaptic transmission
B	1905665	biological_process	positive regulation of calcium ion import across plasma membrane
B	1905949	biological_process	negative regulation of calcium ion import across plasma membrane
C	0016787	molecular_function	hydrolase activity
C	0033192	molecular_function	calmodulin-dependent protein phosphatase activity
C	0097720	biological_process	calcineurin-mediated signaling
D	0004721	molecular_function	phosphoprotein phosphatase activity
D	0004723	molecular_function	calcium-dependent protein serine/threonine phosphatase activity
D	0005509	molecular_function	calcium ion binding
D	0005515	molecular_function	protein binding
D	0005516	molecular_function	calmodulin binding
D	0005654	cellular_component	nucleoplasm
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0005955	cellular_component	calcineurin complex
D	0008287	cellular_component	protein serine/threonine phosphatase complex
D	0008597	molecular_function	calcium-dependent protein serine/threonine phosphatase regulator activity
D	0019902	molecular_function	phosphatase binding
D	0019904	molecular_function	protein domain specific binding
D	0033173	biological_process	calcineurin-NFAT signaling cascade
D	0042383	cellular_component	sarcolemma
D	0045202	cellular_component	synapse
D	0045944	biological_process	positive regulation of transcription by RNA polymerase II
D	0046872	molecular_function	metal ion binding
D	0070886	biological_process	positive regulation of calcineurin-NFAT signaling cascade
D	0098685	cellular_component	Schaffer collateral - CA1 synapse
D	0098686	cellular_component	hippocampal mossy fiber to CA3 synapse
D	0098688	cellular_component	parallel fiber to Purkinje cell synapse
D	0098693	biological_process	regulation of synaptic vesicle cycle
D	0098794	cellular_component	postsynapse
D	0098978	cellular_component	glutamatergic synapse
D	0099149	biological_process	regulation of postsynaptic neurotransmitter receptor internalization
D	0099170	biological_process	postsynaptic modulation of chemical synaptic transmission
D	1905665	biological_process	positive regulation of calcium ion import across plasma membrane
D	1905949	biological_process	negative regulation of calcium ion import across plasma membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN A 509

Chain	Residue
A	ASP118
A	ASN150
A	HIS199
A	HIS281
A	FE510
A	PO4511

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE A 510

Chain	Residue
A	ZN509
A	PO4511
A	HOH673
A	ASP90
A	HIS92
A	ASP118

site_id	AC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PO4 A 511

Chain	Residue
A	HIS92
A	ASP118
A	ARG122
A	ASN150
A	HIS151
A	ARG254
A	HIS281
A	ZN509
A	FE510
A	HOH538
A	HOH554
A	HOH615

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 501

Chain	Residue
B	ASP30
B	ASP32
B	SER34
B	SER36
B	GLU41
B	GLU68

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 502

Chain	Residue
B	ASP62
B	ASP64
B	ASN66
B	GLU68
B	GLU73
B	HOH530

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 503

Chain	Residue
B	ASP99
B	ASP101
B	ASP103
B	TYR105
B	GLU110
B	HOH521

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 504

Chain	Residue
B	ASP140
B	ASP142
B	ASP144
B	ARG146
B	GLU151
B	HOH532

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN C 512

Chain	Residue
C	ASP118
C	ASN150
C	HIS199
C	HIS281
C	FE513
C	PO4514

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE C 513

Chain	Residue
C	ASP90
C	HIS92
C	ASP118
C	ZN512
C	PO4514
C	HOH603

site_id	BC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PO4 C 514

Chain	Residue
C	HIS92
C	ASP118
C	ARG122
C	ASN150
C	HIS151
C	ARG254
C	HIS281
C	ZN512
C	FE513
C	HOH611
C	HOH623

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 505

Chain	Residue
D	ASP30
D	ASP32
D	SER34
D	SER36
D	GLU41
D	HOH533

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 506

Chain	Residue
D	ASP62
D	ASP64
D	ASN66
D	GLU68
D	GLU73
D	HOH528

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 507

Chain	Residue
D	ASP99
D	ASP101
D	ASP103
D	TYR105
D	GLU110
D	HOH523

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 508

Chain	Residue
D	ASP140
D	ASP142
D	ASP144
D	ARG146
D	GLU151
D	HOH530

Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DLDNSGSLSveEF

Chain	Residue	Details
B	ASP30-PHE42
B	ASP62-PHE74
B	ASP99-LEU111
B	ASP140-PHE152

site_id	PS00125
Number of Residues	6
Details	SER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE

Chain	Residue	Details
A	LEU147-GLU152

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	568
Details	Region: {"description":"Catalytic","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	18
Details	Region: {"description":"Interaction with PxIxIF motif in substrate","evidences":[{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17502104","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343722","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26248042","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	56
Details	Region: {"description":"Calcineurin B binding","evidences":[{"source":"PubMed","id":"12218175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12357034","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Motif: {"description":"SAPNY motif","evidences":[{"source":"PubMed","id":"26248042","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12218175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343722","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26248042","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31375679","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AUI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1M63","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2P6B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LL8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5C1V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SVE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NUC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NUU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6UUQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Site: {"description":"Interaction with PxVP motif in substrate","evidences":[{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P63328","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	56
Details	Domain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	70
Details	Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	70
Details	Domain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	10
Details	Region: {"description":"Calcineurin A binding","evidences":[{"source":"PubMed","id":"12218175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12357034","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343722","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26794871","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	30
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12218175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12357034","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343722","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26794871","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AUI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1M63","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1MF8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2P6B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LL8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4F0Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4OR9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ORA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ORC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SVE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12218175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12357034","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343722","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26794871","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31375679","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NUC","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"1AUI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1M63","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1MF8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2P6B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LL8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4F0Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4OR9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ORA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ORC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SVE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	4
Details	Site: {"description":"Interaction with PxVP motif in substrates of the catalytic subunit","evidences":[{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q63810","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	35
Details	Domain: {"description":"EF-hand 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1aui

Chain	Residue	Details
A	ASP121
A	HIS151

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1aui

Chain	Residue	Details
C	ASP121
C	HIS151

site_id	MCSA1
Number of Residues	10
Details	M-CSA 406

Chain	Residue	Details
B	ILE106	metal ligand
B	ASN108	metal ligand
B	LYS134	metal ligand
B	ILE137	electrostatic stabiliser
B	ASN138	transition state stabiliser
B	VAL166	metal ligand
B	VAL167	proton shuttle (general acid/base)

site_id	MCSA2
Number of Residues	10
Details	M-CSA 406

Chain	Residue	Details
D	ILE106	metal ligand
D	ASN108	metal ligand
D	LYS134	metal ligand
D	ILE137	electrostatic stabiliser
D	ASN138	transition state stabiliser
D	VAL166	metal ligand
D	VAL167	proton shuttle (general acid/base)

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)