1CDM

MODULATION OF CALMODULIN PLASTICITY IN MOLECULAR RECOGNITION ON THE BASIS OF X-RAY STRUCTURES

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000922	cellular_component	spindle pole
A	0005509	molecular_function	calcium ion binding
A	0005513	biological_process	detection of calcium ion
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005813	cellular_component	centrosome
A	0005819	cellular_component	spindle
A	0005829	cellular_component	cytosol
A	0010880	biological_process	regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
A	0019904	molecular_function	protein domain specific binding
A	0030672	cellular_component	synaptic vesicle membrane
A	0032991	cellular_component	protein-containing complex
A	0043209	cellular_component	myelin sheath
A	0046872	molecular_function	metal ion binding
A	0097720	biological_process	calcineurin-mediated signaling

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 1

Chain	Residue
A	ASP20
A	ASP22
A	ASP24
A	THR26
A	GLU31
A	HOH186

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 2

Chain	Residue
A	THR62
A	GLU67
A	HOH189
A	ASP56
A	ASP58
A	ASN60

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 3

Chain	Residue
A	ASP93
A	ASP95
A	ASN97
A	TYR99
A	GLU104
A	HOH158

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 148

Chain	Residue
A	ASP129
A	ASP131
A	ASP133
A	GLN135
A	GLU140
A	HOH179

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASP20-LEU32
A	ASP56-PHE68
A	ASP93-LEU105
A	ASP129-PHE141

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	35
Details	Domain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by CaMK4","evidences":[{"source":"UniProtKB","id":"P0DP29","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"9716384","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---