Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2DG1

Crystal structure of Drp35, a 35kDa drug responsive protein from Staphylococcus aureus, complexed with Ca2+

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding
B	0005737	cellular_component	cytoplasm
B	0016787	molecular_function	hydrolase activity
B	0046872	molecular_function	metal ion binding
C	0005737	cellular_component	cytoplasm
C	0016787	molecular_function	hydrolase activity
C	0046872	molecular_function	metal ion binding
D	0005737	cellular_component	cytoplasm
D	0016787	molecular_function	hydrolase activity
D	0046872	molecular_function	metal ion binding
E	0005737	cellular_component	cytoplasm
E	0016787	molecular_function	hydrolase activity
E	0046872	molecular_function	metal ion binding
F	0005737	cellular_component	cytoplasm
F	0016787	molecular_function	hydrolase activity
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CA A 3001

Chain	Residue
A	GLU48
A	ASP138
A	ASN185
A	ASP236
A	SER237
A	HOH5068
A	HOH5220
A	HOH5221

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CA B 3002

Chain	Residue
B	ASP138
B	ASN185
B	ASP236
B	SER237
B	HOH5029
B	HOH5221
B	HOH5222
B	GLU48

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CA C 3003

Chain	Residue
C	GLU48
C	ASP138
C	ASN185
C	ASP236
C	SER237
C	HOH5049
C	HOH5212
C	HOH5213

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CA D 3004

Chain	Residue
D	GLU48
D	ASP138
D	ASN185
D	ASP236
D	SER237
D	HOH5029
D	HOH5230
D	HOH5231

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CA E 3005

Chain	Residue
E	GLU48
E	ASP138
E	ASN185
E	ASP236
E	SER237
E	HOH5024
E	HOH5235
E	HOH5236

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CA F 3006

Chain	Residue
F	GLU48
F	ASP138
F	ASN185
F	ASP236
F	SER237
F	HOH5064
F	HOH5203
F	HOH5204

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 3007

Chain	Residue
A	SER110
A	GLY112
A	ASP130
A	THR133
A	TYR135
A	HOH5293

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 3008

Chain	Residue
B	SER110
B	GLY112
B	ASP130
B	THR133
B	TYR135

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA C 3009

Chain	Residue
C	SER110
C	GLY112
C	ASP130
C	THR133
C	TYR135

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA D 3010

Chain	Residue
D	SER110
D	GLY112
D	ASP130
D	THR133
D	TYR135

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA E 3011

Chain	Residue
E	SER110
E	GLY112
E	ASP130
E	THR133
E	TYR135

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA F 3012

Chain	Residue
F	SER110
F	GLY112
F	ASP130
F	THR133
F	TYR135

site_id	BC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 5001

Chain	Residue
A	CYS239
A	ILE240
A	GLN286
A	PHE287
A	GLY318
A	HIS319
A	HOH5053
A	HOH5055

site_id	BC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL B 5002

Chain	Residue
B	CYS239
B	ILE240
B	GLN286
B	PHE287
B	GLY318
B	HIS319
B	HOH5017
B	HOH5373

site_id	BC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL C 5003

Chain	Residue
C	GLY318
C	HIS319
C	HOH5046
C	HOH5072
C	CYS239
C	ILE240
C	GLN286
C	PHE287

site_id	BC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL D 5004

Chain	Residue
D	CYS239
D	ILE240
D	GLN286
D	PHE287
D	GLY318
D	HIS319
D	HOH5035
D	HOH5072

site_id	BC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL E 5005

Chain	Residue
E	CYS239
E	ILE240
E	GLN286
E	PHE287
E	GLY318
E	HIS319
E	HOH5055
E	HOH5080

site_id	BC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL F 5006

Chain	Residue
F	CYS239
F	ILE240
F	GLN286
F	PHE287
F	HIS319
F	HOH5051
F	HOH5345

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 5007

Chain	Residue
A	LYS16
A	HOH5076
B	SER27
B	HOH5147
B	HOH5240
B	HOH5300

site_id	CC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 5008

Chain	Residue
B	LYS16
B	ILE23
B	HOH5055
B	HOH5225
C	SER27
C	THR31

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL C 5009

Chain	Residue
A	SER27
A	HOH5061
A	HOH5225
C	LYS16
C	HOH5066

site_id	CC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 5010

Chain	Residue
D	LYS16
D	ILE23
D	HOH5031
F	SER27
F	THR31
F	HOH5211

site_id	CC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL E 5011

Chain	Residue
D	SER27
D	HOH5117
D	HOH5296
E	LYS16
E	ILE23
E	HOH5046

site_id	CC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL F 5012

Chain	Residue
E	SER27
E	HOH5098
E	HOH5214
F	LYS16
F	HOH5059
F	HOH5237

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: Proton donor => ECO:0000255

Chain	Residue	Details
A	ASP236
B	ASP236
C	ASP236
D	ASP236
E	ASP236
F	ASP236

site_id	SWS_FT_FI2
Number of Residues	60
Details	BINDING:

Chain	Residue	Details
A	GLU48
A	SER237
B	GLU48
B	SER110
B	GLY112
B	ASP130
B	THR133
B	TYR135
B	ASP138
B	ASN185
B	ASP236
A	SER110
B	SER237
C	GLU48
C	SER110
C	GLY112
C	ASP130
C	THR133
C	TYR135
C	ASP138
C	ASN185
C	ASP236
A	GLY112
C	SER237
D	GLU48
D	SER110
D	GLY112
D	ASP130
D	THR133
D	TYR135
D	ASP138
D	ASN185
D	ASP236
A	ASP130
D	SER237
E	GLU48
E	SER110
E	GLY112
E	ASP130
E	THR133
E	TYR135
E	ASP138
E	ASN185
E	ASP236
A	THR133
E	SER237
F	GLU48
F	SER110
F	GLY112
F	ASP130
F	THR133
F	TYR135
F	ASP138
F	ASN185
F	ASP236
A	TYR135
F	SER237
A	ASP138
A	ASN185
A	ASP236

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