Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7EG2

Crystal structure of the apoAequorin complex with (S)-daCTZ

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005509	molecular_function	calcium ion binding
A	0008218	biological_process	bioluminescence
A	0046872	molecular_function	metal ion binding
B	0005509	molecular_function	calcium ion binding
B	0008218	biological_process	bioluminescence
B	0046872	molecular_function	metal ion binding
C	0005509	molecular_function	calcium ion binding
C	0008218	biological_process	bioluminescence
C	0046872	molecular_function	metal ion binding
D	0005509	molecular_function	calcium ion binding
D	0008218	biological_process	bioluminescence
D	0046872	molecular_function	metal ion binding
E	0005509	molecular_function	calcium ion binding
E	0008218	biological_process	bioluminescence
E	0046872	molecular_function	metal ion binding
F	0005509	molecular_function	calcium ion binding
F	0008218	biological_process	bioluminescence
F	0046872	molecular_function	metal ion binding
G	0005509	molecular_function	calcium ion binding
G	0008218	biological_process	bioluminescence
G	0046872	molecular_function	metal ion binding
H	0005509	molecular_function	calcium ion binding
H	0008218	biological_process	bioluminescence
H	0046872	molecular_function	metal ion binding
I	0005509	molecular_function	calcium ion binding
I	0008218	biological_process	bioluminescence
I	0046872	molecular_function	metal ion binding
J	0005509	molecular_function	calcium ion binding
J	0008218	biological_process	bioluminescence
J	0046872	molecular_function	metal ion binding
K	0005509	molecular_function	calcium ion binding
K	0008218	biological_process	bioluminescence
K	0046872	molecular_function	metal ion binding
L	0005509	molecular_function	calcium ion binding
L	0008218	biological_process	bioluminescence
L	0046872	molecular_function	metal ion binding
M	0005509	molecular_function	calcium ion binding
M	0008218	biological_process	bioluminescence
M	0046872	molecular_function	metal ion binding
N	0005509	molecular_function	calcium ion binding
N	0008218	biological_process	bioluminescence
N	0046872	molecular_function	metal ion binding
O	0005509	molecular_function	calcium ion binding
O	0008218	biological_process	bioluminescence
O	0046872	molecular_function	metal ion binding
P	0005509	molecular_function	calcium ion binding
P	0008218	biological_process	bioluminescence
P	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	binding site for residue J2X A 201

Chain	Residue
A	HIS16
A	TRP108
A	GLY109
A	LEU112
A	PHE113
A	TYR132
A	ILE138
A	MET165
A	HIS169
A	TRP173
A	TYR184
A	MET19
A	HOH307
A	LEU23
A	MET36
A	LYS39
A	ALA40
A	TYR82
A	TRP86
A	ILE105

site_id	AC2
Number of Residues	18
Details	binding site for residue J2X B 201

Chain	Residue
B	HIS16
B	MET19
B	LYS39
B	ALA40
B	TYR82
B	TRP86
B	ILE105
B	TRP108
B	GLY109
B	LEU112
B	PHE113
B	TRP129
B	TYR132
B	ILE138
B	HIS169
B	TRP173
B	TYR184
B	HOH302

site_id	AC3
Number of Residues	19
Details	binding site for residue J2X C 201

Chain	Residue
C	HIS16
C	MET19
C	LEU23
C	MET36
C	LYS39
C	ALA40
C	TYR82
C	TRP86
C	ILE105
C	TRP108
C	GLY109
C	LEU112
C	PHE113
C	TYR132
C	ILE138
C	HIS169
C	TRP173
C	TYR184
C	HOH308

site_id	AC4
Number of Residues	20
Details	binding site for residue J2X D 201

Chain	Residue
D	HIS16
D	MET19
D	LEU23
D	MET36
D	LYS39
D	ALA40
D	TYR82
D	TRP86
D	ILE105
D	TRP108
D	GLY109
D	LEU112
D	PHE113
D	TYR132
D	ILE138
D	MET165
D	HIS169
D	TRP173
D	TYR184
D	HOH301

site_id	AC5
Number of Residues	20
Details	binding site for residue J2X E 201

Chain	Residue
E	HIS16
E	MET19
E	LEU23
E	MET36
E	LYS39
E	ALA40
E	TYR82
E	TRP86
E	ILE105
E	TRP108
E	GLY109
E	LEU112
E	PHE113
E	TRP129
E	TYR132
E	ILE138
E	HIS169
E	TRP173
E	TYR184
E	HOH305

site_id	AC6
Number of Residues	18
Details	binding site for residue J2X F 201

Chain	Residue
F	LEU23
F	LYS39
F	ALA40
F	TYR82
F	TRP86
F	ILE105
F	TRP108
F	GLY109
F	LEU112
F	PHE113
F	TYR132
F	ILE138
F	HIS169
F	TRP173
F	TYR184
F	HOH304
F	HIS16
F	MET19

site_id	AC7
Number of Residues	20
Details	binding site for residue J2X G 201

Chain	Residue
G	HIS16
G	MET19
G	LEU23
G	MET36
G	LYS39
G	ALA40
G	PHE66
G	TYR82
G	TRP86
G	ILE105
G	TRP108
G	GLY109
G	LEU112
G	PHE113
G	TYR132
G	ILE138
G	HIS169
G	TRP173
G	TYR184
G	HOH314

site_id	AC8
Number of Residues	20
Details	binding site for residue J2X H 201

Chain	Residue
H	HIS16
H	MET19
H	LEU23
H	MET36
H	LYS39
H	ALA40
H	PHE66
H	TYR82
H	TRP86
H	ILE105
H	TRP108
H	GLY109
H	LEU112
H	PHE113
H	TYR132
H	ILE138
H	HIS169
H	TRP173
H	TYR184
H	HOH304

site_id	AC9
Number of Residues	21
Details	binding site for residue J2X I 201

Chain	Residue
I	HIS16
I	MET19
I	LEU23
I	MET36
I	LYS39
I	ALA40
I	TYR82
I	TRP86
I	ILE105
I	TRP108
I	GLY109
I	LEU112
I	PHE113
I	TRP129
I	TYR132
I	ILE138
I	MET165
I	HIS169
I	TRP173
I	TYR184
I	HOH301

site_id	AD1
Number of Residues	18
Details	binding site for residue J2X J 201

Chain	Residue
J	HIS16
J	MET19
J	MET36
J	LYS39
J	ALA40
J	TYR82
J	TRP86
J	ILE105
J	TRP108
J	GLY109
J	LEU112
J	PHE113
J	TYR132
J	ILE138
J	HIS169
J	TRP173
J	TYR184
J	HOH305

site_id	AD2
Number of Residues	20
Details	binding site for residue J2X K 201

Chain	Residue
K	HIS16
K	MET19
K	LEU23
K	MET36
K	LYS39
K	ALA40
K	PHE66
K	TYR82
K	TRP86
K	ILE105
K	TRP108
K	GLY109
K	LEU112
K	PHE113
K	TRP129
K	TYR132
K	HIS169
K	TRP173
K	TYR184
K	HOH307

site_id	AD3
Number of Residues	19
Details	binding site for residue J2X L 201

Chain	Residue
L	HIS16
L	MET19
L	MET36
L	ALA40
L	PHE66
L	TYR82
L	TRP86
L	ILE105
L	TRP108
L	GLY109
L	LEU112
L	PHE113
L	TYR132
L	ILE138
L	MET165
L	HIS169
L	TRP173
L	TYR184
L	HOH305

site_id	AD4
Number of Residues	19
Details	binding site for residue J2X M 201

Chain	Residue
M	HIS16
M	MET19
M	LEU23
M	MET36
M	LYS39
M	ALA40
M	TYR82
M	TRP86
M	ILE105
M	TRP108
M	GLY109
M	LEU112
M	PHE113
M	TYR132
M	ILE138
M	HIS169
M	TRP173
M	TYR184
M	HOH304

site_id	AD5
Number of Residues	19
Details	binding site for residue J2X N 201

Chain	Residue
N	HIS16
N	MET19
N	LEU23
N	LYS39
N	ALA40
N	TYR82
N	TRP86
N	ILE105
N	TRP108
N	GLY109
N	LEU112
N	PHE113
N	TYR132
N	ILE138
N	MET165
N	HIS169
N	TRP173
N	TYR184
N	HOH305

site_id	AD6
Number of Residues	19
Details	binding site for residue J2X O 201

Chain	Residue
O	HIS16
O	MET19
O	LEU23
O	MET36
O	LYS39
O	ALA40
O	TYR82
O	TRP86
O	ILE105
O	TRP108
O	GLY109
O	LEU112
O	PHE113
O	TYR132
O	ILE138
O	HIS169
O	TRP173
O	TYR184
O	HOH311

site_id	AD7
Number of Residues	20
Details	binding site for residue J2X P 201

Chain	Residue
P	HIS16
P	MET19
P	LEU23
P	MET36
P	LYS39
P	ALA40
P	TYR82
P	TRP86
P	ILE105
P	TRP108
P	GLY109
P	LEU112
P	PHE113
P	TYR132
P	ILE138
P	MET165
P	HIS169
P	TRP173
P	TYR184
P	HOH307

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASP24-MET36
A	ASP117-TRP129
A	ASP153-MET165

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	224
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00448

Chain	Residue	Details
A	ASP24
A	ASN26
A	ASN28
A	LYS30
A	GLU35
F	ASP155
F	SER157
F	GLN159
F	GLU164
G	ASP24
G	ASN26
G	ASN28
G	LYS30
G	GLU35
G	ASP117
G	ASP119
G	ASN121
G	GLU128
G	ASP153
G	ASP155
G	SER157
G	GLN159
G	GLU164
H	ASP24
H	ASN26
H	ASN28
H	LYS30
H	GLU35
H	ASP117
H	ASP119
H	ASN121
H	GLU128
H	ASP153
H	ASP155
H	SER157
H	GLN159
H	GLU164
I	ASP24
I	ASN26
I	ASN28
I	LYS30
I	GLU35
I	ASP117
I	ASP119
I	ASN121
I	GLU128
I	ASP153
I	ASP155
I	SER157
I	GLN159
I	GLU164
J	ASP24
J	ASN26
J	ASN28
J	LYS30
J	GLU35
J	ASP117
J	ASP119
J	ASN121
J	GLU128
J	ASP153
J	ASP155
J	SER157
J	GLN159
J	GLU164
K	ASP24
K	ASN26
K	ASN28
K	LYS30
K	GLU35
K	ASP117
K	ASP119
K	ASN121
K	GLU128
K	ASP153
K	ASP155
K	SER157
K	GLN159
K	GLU164
L	ASP24
L	ASN26
L	ASN28
L	LYS30
L	GLU35
L	ASP117
L	ASP119
L	ASN121
L	GLU128
L	ASP153
L	ASP155
L	SER157
L	GLN159
L	GLU164
M	ASP24
M	ASN26
M	ASN28
M	LYS30
M	GLU35
M	ASP117
M	ASP119
M	ASN121
M	GLU128
M	ASP153
M	ASP155
M	SER157
M	GLN159
M	GLU164
N	ASP24
N	ASN26
N	ASN28
N	LYS30
N	GLU35
N	ASP117
N	ASP119
N	ASN121
N	GLU128
N	ASP153
N	ASP155
N	SER157
N	GLN159
N	GLU164
O	ASP24
O	ASN26
O	ASN28
O	LYS30
O	GLU35
O	ASP117
O	ASP119
O	ASN121
O	GLU128
O	ASP153
O	ASP155
O	SER157
O	GLN159
O	GLU164
P	ASP24
P	ASN26
P	ASN28
P	LYS30
P	GLU35
P	ASP117
P	ASP119
P	ASN121
P	GLU128
P	ASP153
P	ASP155
P	SER157
P	GLN159
P	GLU164
A	ASP117
A	ASP119
A	ASN121
A	GLU128
A	ASP153
A	ASP155
A	SER157
A	GLN159
A	GLU164
B	ASP24
B	ASN26
B	ASN28
B	LYS30
B	GLU35
B	ASP117
B	ASP119
B	ASN121
B	GLU128
B	ASP153
B	ASP155
B	SER157
B	GLN159
B	GLU164
C	ASP24
C	ASN26
C	ASN28
C	LYS30
C	GLU35
C	ASP117
C	ASP119
C	ASN121
C	GLU128
C	ASP153
C	ASP155
C	SER157
C	GLN159
C	GLU164
D	ASP24
D	ASN26
D	ASN28
D	LYS30
D	GLU35
D	ASP117
D	ASP119
D	ASN121
D	GLU128
D	ASP153
D	ASP155
D	SER157
D	GLN159
D	GLU164
E	ASP24
E	ASN26
E	ASN28
E	LYS30
E	GLU35
E	ASP117
E	ASP119
E	ASN121
E	GLU128
E	ASP153
E	ASP155
E	SER157
E	GLN159
E	GLU164
F	ASP24
F	ASN26
F	ASN28
F	LYS30
F	GLU35
F	ASP117
F	ASP119
F	ASN121
F	GLU128
F	ASP153

site_id	SWS_FT_FI2
Number of Residues	16
Details	SITE: Required for bioluminescence

Chain	Residue	Details
A	PRO189
B	PRO189
C	PRO189
D	PRO189
E	PRO189
F	PRO189
G	PRO189
H	PRO189
I	PRO189
J	PRO189
K	PRO189
L	PRO189
M	PRO189
N	PRO189
O	PRO189
P	PRO189

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