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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3EKH

Calcium-saturated GCaMP2 T116V/K378W mutant monomer

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005509	molecular_function	calcium ion binding
A	0006091	biological_process	generation of precursor metabolites and energy
A	0008218	biological_process	bioluminescence

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 452

Chain	Residue
A	ASP261
A	ASP287
A	SER320
A	ASP323
A	GLY326
A	HOH476
A	HOH635

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 453

Chain	Residue
A	ASP327
A	THR329
A	GLU334
A	HOH536
A	ASP323
A	ASP325

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 454

Chain	Residue
A	ASP359
A	ASP361
A	ASN363
A	THR365
A	ASP367
A	GLU370

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 455

Chain	Residue
A	ASP396
A	ASP398
A	ASN400
A	TYR402
A	GLU407

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 456

Chain	Residue
A	ASP432
A	ASP434
A	ASP436
A	GLN438
A	GLU443

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	ASP325-THR337
A	ASP361-THR373
A	ASP398-HIS410
A	ASP434-GLN446

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: (Z)-2,3-didehydrotyrosine => ECO:0000269\|PubMed:8448132

Chain	Residue	Details
A	VAL226

site_id	SWS_FT_FI2
Number of Residues	2
Details	CROSSLNK: 5-imidazolinone (Ser-Gly) => ECO:0000269\|PubMed:8448132

Chain	Residue	Details
A	CRO224
A	GLN227

site_id	SWS_FT_FI3
Number of Residues	5
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00448, ECO:0000269\|PubMed:23109337, ECO:0000269\|PubMed:3145979, ECO:0007744\|PDB:1G4Y, ECO:0007744\|PDB:1NIW, ECO:0007744\|PDB:2HQW, ECO:0007744\|PDB:2YGG, ECO:0007744\|PDB:3B32, ECO:0007744\|PDB:3BXK, ECO:0007744\|PDB:3BXL, ECO:0007744\|PDB:3CLN, ECO:0007744\|PDB:3IFK, ECO:0007744\|PDB:3SJQ, ECO:0007744\|PDB:4EHQ, ECO:0007744\|PDB:4G27, ECO:0007744\|PDB:4G28, ECO:0007744\|PDB:4I2Y, ECO:0007744\|PDB:4J9Y, ECO:0007744\|PDB:4J9Z, ECO:0007744\|PDB:4QNH

Chain	Residue	Details
A	ASP323
A	ASP325
A	ASP327
A	THR329
A	GLU334

Chain	Residue	Details
A	ASP359
A	ASP361
A	ASN363
A	THR365
A	GLU370

site_id	SWS_FT_FI5
Number of Residues	5
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00448, ECO:0000269\|PubMed:23109337, ECO:0000269\|PubMed:3145979, ECO:0007744\|PDB:1NIW, ECO:0007744\|PDB:2HQW, ECO:0007744\|PDB:2YGG, ECO:0007744\|PDB:3BXK, ECO:0007744\|PDB:3BXL, ECO:0007744\|PDB:3CLN, ECO:0007744\|PDB:3EK4, ECO:0007744\|PDB:3EK7, ECO:0007744\|PDB:3EK8, ECO:0007744\|PDB:3EKH, ECO:0007744\|PDB:3EVR, ECO:0007744\|PDB:3EVU, ECO:0007744\|PDB:3SG2, ECO:0007744\|PDB:3SG3, ECO:0007744\|PDB:3SG4, ECO:0007744\|PDB:3SG5, ECO:0007744\|PDB:3SG6, ECO:0007744\|PDB:3SG7, ECO:0007744\|PDB:3SJQ, ECO:0007744\|PDB:3WLC, ECO:0007744\|PDB:3WLD, ECO:0007744\|PDB:4EHQ, ECO:0007744\|PDB:4I2Y, ECO:0007744\|PDB:4RJD

Chain	Residue	Details
A	ASP396
A	ASP398
A	ASN400
A	TYR402
A	GLU407

site_id	SWS_FT_FI6
Number of Residues	5
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00448, ECO:0000269\|PubMed:23109337, ECO:0000269\|PubMed:3145979, ECO:0007744\|PDB:1NIW, ECO:0007744\|PDB:2HQW, ECO:0007744\|PDB:2YGG, ECO:0007744\|PDB:3BXK, ECO:0007744\|PDB:3BXL, ECO:0007744\|PDB:3CLN, ECO:0007744\|PDB:3EK7, ECO:0007744\|PDB:3EK8, ECO:0007744\|PDB:3EKH, ECO:0007744\|PDB:3EVR, ECO:0007744\|PDB:3EVU, ECO:0007744\|PDB:3SG2, ECO:0007744\|PDB:3SG3, ECO:0007744\|PDB:3SG4, ECO:0007744\|PDB:3SG5, ECO:0007744\|PDB:3SG7, ECO:0007744\|PDB:3SJQ, ECO:0007744\|PDB:3WLC, ECO:0007744\|PDB:3WLD, ECO:0007744\|PDB:4EHQ, ECO:0007744\|PDB:4I2Y, ECO:0007744\|PDB:4RJD

Chain	Residue	Details
A	ASP432
A	ASP434
A	ASP436
A	GLN438
A	GLU443

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0000250\|UniProtKB:P0DP23

Chain	Residue	Details
A	LYS324

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by CaMK4 => ECO:0000269\|PubMed:12392717

Chain	Residue	Details
A	THR347

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P0DP23

Chain	Residue	Details
A	SER384

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P0DP23

Chain	Residue	Details
A	LYS397

site_id	SWS_FT_FI11
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0007744\|PubMed:22673903

Chain	Residue	Details
A	TYR402

site_id	SWS_FT_FI12
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:22673903

Chain	Residue	Details
A	SER404

site_id	SWS_FT_FI13
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:P0DP23

Chain	Residue	Details
A	THR413

site_id	SWS_FT_FI14
Number of Residues	1
Details	MOD_RES: N6-methyllysine; alternate => ECO:0000250\|UniProtKB:P0DP23

Chain	Residue	Details
A	LYS418

site_id	SWS_FT_FI15
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250\|UniProtKB:P0DP23

Chain	Residue	Details
A	TYR441

site_id	SWS_FT_FI16
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250\|UniProtKB:P62157

Chain	Residue	Details
A	LYS324

site_id	SWS_FT_FI17
Number of Residues	1
Details	MOD_RES: Phosphoserine; by PKG => ECO:0000269\|PubMed:12176732

Chain	Residue	Details
A	ASN72

218853

PDB entries from 2024-04-24

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