Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6HVQ

The structure of Dps from Listeria innocua soaked before soaking experiments with Zn, Co and La

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0006879	biological_process	intracellular iron ion homeostasis
A	0008199	molecular_function	ferric iron binding
A	0016491	molecular_function	oxidoreductase activity
A	0016722	molecular_function	oxidoreductase activity, acting on metal ions
A	0046872	molecular_function	metal ion binding
B	0005737	cellular_component	cytoplasm
B	0006879	biological_process	intracellular iron ion homeostasis
B	0008199	molecular_function	ferric iron binding
B	0016491	molecular_function	oxidoreductase activity
B	0016722	molecular_function	oxidoreductase activity, acting on metal ions
B	0046872	molecular_function	metal ion binding
C	0005737	cellular_component	cytoplasm
C	0006879	biological_process	intracellular iron ion homeostasis
C	0008199	molecular_function	ferric iron binding
C	0016491	molecular_function	oxidoreductase activity
C	0016722	molecular_function	oxidoreductase activity, acting on metal ions
C	0046872	molecular_function	metal ion binding
D	0005737	cellular_component	cytoplasm
D	0006879	biological_process	intracellular iron ion homeostasis
D	0008199	molecular_function	ferric iron binding
D	0016491	molecular_function	oxidoreductase activity
D	0016722	molecular_function	oxidoreductase activity, acting on metal ions
D	0046872	molecular_function	metal ion binding
E	0005737	cellular_component	cytoplasm
E	0006879	biological_process	intracellular iron ion homeostasis
E	0008199	molecular_function	ferric iron binding
E	0016491	molecular_function	oxidoreductase activity
E	0016722	molecular_function	oxidoreductase activity, acting on metal ions
E	0046872	molecular_function	metal ion binding
F	0005737	cellular_component	cytoplasm
F	0006879	biological_process	intracellular iron ion homeostasis
F	0008199	molecular_function	ferric iron binding
F	0016491	molecular_function	oxidoreductase activity
F	0016722	molecular_function	oxidoreductase activity, acting on metal ions
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue LA A 201

Chain	Residue
A	ASP130
A	HOH375
C	ASP130
C	HOH359
E	ASP130
E	HOH398

site_id	AC2
Number of Residues	7
Details	binding site for residue LA A 202

Chain	Residue
B	HOH312
B	HOH326
B	HOH353
C	HOH392
A	ASP58
A	GLU62
B	HIS31

site_id	AC3
Number of Residues	8
Details	binding site for residue LA A 203

Chain	Residue
A	ASN5
A	SER6
A	GLU11
A	HOH306
A	HOH339
A	HOH351
A	HOH358
A	HOH374

site_id	AC4
Number of Residues	5
Details	binding site for residue LA A 204

Chain	Residue
A	GLU118
A	LA205
A	HOH367
A	HOH412
E	HOH326

site_id	AC5
Number of Residues	6
Details	binding site for residue LA A 205

Chain	Residue
A	ASP121
A	LA204
A	HOH435
E	LA204
E	HOH326
E	HOH350

site_id	AC6
Number of Residues	6
Details	binding site for residue LA A 206

Chain	Residue
A	GLU44
A	HOH362
A	HOH399
D	LA205
D	HOH454
F	LA205

site_id	AC7
Number of Residues	8
Details	binding site for residue LA A 207

Chain	Residue
A	ASP121
A	HOH303
A	HOH305
A	HOH354
A	HOH431
A	HOH436
C	LA206
E	HOH432

site_id	AC8
Number of Residues	7
Details	binding site for residue LA A 208

Chain	Residue
A	ASP58
A	LA209
A	HOH401
A	HOH427
C	HOH392
C	HOH398
C	HOH444

site_id	AC9
Number of Residues	4
Details	binding site for residue LA A 209

Chain	Residue
A	LA208
A	HOH401
A	HOH432
C	HOH398

site_id	AD1
Number of Residues	7
Details	binding site for residue LA B 201

Chain	Residue
A	HIS31
A	HOH304
A	HOH342
B	ASP58
B	GLU62
B	HOH350
B	HOH390

site_id	AD2
Number of Residues	6
Details	binding site for residue LA B 202

Chain	Residue
B	SER6
B	GLU11
B	HOH306
B	HOH310
B	HOH383
B	HOH392

site_id	AD3
Number of Residues	5
Details	binding site for residue LA B 203

Chain	Residue
B	HIS37
C	ASP96
C	HOH326
C	HOH332
D	HOH401

site_id	AD4
Number of Residues	6
Details	binding site for residue LA B 204

Chain	Residue
B	GLU44
B	LA205
B	HOH391
B	HOH427
C	LA205
E	HOH343

site_id	AD5
Number of Residues	6
Details	binding site for residue LA B 205

Chain	Residue
B	LA204
B	HOH427
C	LA205
E	GLU44
E	HOH301
E	HOH343

site_id	AD6
Number of Residues	5
Details	binding site for residue LA B 206

Chain	Residue
B	ASP58
B	LA208
B	HOH390
B	HOH410
D	HOH421

site_id	AD7
Number of Residues	2
Details	binding site for residue LA B 207

Chain	Residue
B	GLU59
B	LA208

site_id	AD8
Number of Residues	4
Details	binding site for residue LA B 208

Chain	Residue
B	GLU59
B	LA206
B	LA207
D	HOH421

site_id	AD9
Number of Residues	7
Details	binding site for residue LA C 201

Chain	Residue
C	ASP58
C	GLU62
C	HOH307
C	HOH352
C	HOH355
E	HOH397
C	HIS31

site_id	AE1
Number of Residues	8
Details	binding site for residue LA C 202

Chain	Residue
C	GLU100
C	HOH347
C	HOH365
C	HOH403
F	GLU118
F	HOH302
F	HOH391
F	HOH419

site_id	AE2
Number of Residues	8
Details	binding site for residue LA C 203

Chain	Residue
A	HOH310
A	HOH420
C	GLU118
C	LA206
C	HOH311
C	HOH322
C	HOH331
C	HOH424

site_id	AE3
Number of Residues	7
Details	binding site for residue LA C 204

Chain	Residue
A	HOH391
C	SER6
C	GLU11
C	HOH327
C	HOH391
C	HOH415
C	HOH427

site_id	AE4
Number of Residues	6
Details	binding site for residue LA C 205

Chain	Residue
B	LA204
B	LA205
B	HOH391
C	GLU44
C	HOH302
C	HOH353

site_id	AE5
Number of Residues	10
Details	binding site for residue LA C 206

Chain	Residue
A	LA207
A	HOH303
A	HOH310
A	HOH326
A	HOH420
C	ASP121
C	LA203
C	HOH311
C	HOH423
C	HOH448

site_id	AE6
Number of Residues	8
Details	binding site for residue LA C 207

Chain	Residue
C	ASP121
C	HOH301
C	HOH402
C	HOH406
C	HOH429
E	LA203
E	HOH303
E	HOH432

site_id	AE7
Number of Residues	3
Details	binding site for residue LA C 208

Chain	Residue
C	ASP58
C	LA209
E	HOH400

site_id	AE8
Number of Residues	3
Details	binding site for residue LA C 209

Chain	Residue
C	GLU59
C	LA208
E	HOH400

site_id	AE9
Number of Residues	7
Details	binding site for residue LA D 201

Chain	Residue
D	HIS31
D	ASP58
D	GLU62
D	HOH312
D	HOH355
D	HOH384
D	HOH387

site_id	AF1
Number of Residues	7
Details	binding site for residue LA D 202

Chain	Residue
B	HOH308
D	GLU118
D	HOH303
D	HOH349
D	HOH392
D	HOH430
E	HOH428

site_id	AF2
Number of Residues	6
Details	binding site for residue LA D 203

Chain	Residue
B	HOH313
D	SER6
D	GLU11
D	HOH398
D	HOH422
D	HOH423

site_id	AF3
Number of Residues	7
Details	binding site for residue LA D 204

Chain	Residue
D	ASP96
D	GLU100
D	LA206
D	HOH348
D	HOH413
E	HOH302
E	HOH420

site_id	AF4
Number of Residues	8
Details	binding site for residue LA D 205

Chain	Residue
A	LA206
A	HOH362
D	GLU44
D	HOH302
D	HOH418
D	HOH454
F	LA205
F	HOH429

site_id	AF5
Number of Residues	6
Details	binding site for residue LA D 206

Chain	Residue
D	GLU100
D	LA204
D	HOH348
D	HOH433
E	HOH302
E	HOH420

site_id	AF6
Number of Residues	5
Details	binding site for residue LA D 207

Chain	Residue
D	GLU85
D	HOH325
D	HOH424
D	HOH439
D	HOH450

site_id	AF7
Number of Residues	4
Details	binding site for residue LA D 208

Chain	Residue
D	GLU85
D	HOH325
D	HOH427
D	HOH457

site_id	AF8
Number of Residues	7
Details	binding site for residue LA E 201

Chain	Residue
E	ASP58
E	GLU62
E	HOH367
E	HOH369
F	HIS31
F	HOH326
F	HOH333

site_id	AF9
Number of Residues	7
Details	binding site for residue LA E 202

Chain	Residue
C	HOH316
C	HOH438
E	GLU118
E	LA203
E	HOH317
E	HOH333
E	HOH411

site_id	AG1
Number of Residues	8
Details	binding site for residue LA E 203

Chain	Residue
C	LA207
C	HOH301
C	HOH316
C	HOH402
E	ASP121
E	LA202
E	HOH413
E	HOH435

site_id	AG2
Number of Residues	7
Details	binding site for residue LA E 204

Chain	Residue
A	LA205
A	HOH305
A	HOH436
E	ASP121
E	HOH303
E	HOH424
E	HOH432

site_id	AG3
Number of Residues	5
Details	binding site for residue LA E 205

Chain	Residue
A	HOH406
E	ASP58
E	HOH367
E	HOH431
E	HOH436

site_id	AG4
Number of Residues	2
Details	binding site for residue LA E 206

Chain	Residue
E	GLU85
E	HOH412

site_id	AG5
Number of Residues	7
Details	binding site for residue LA F 201

Chain	Residue
E	HIS31
E	HOH321
E	HOH351
E	HOH381
F	ASP58
F	GLU62
F	HOH415

site_id	AG6
Number of Residues	6
Details	binding site for residue LA F 202

Chain	Residue
B	ASP130
B	HOH369
B	HOH400
D	ASP130
D	HOH365
F	ASP130

site_id	AG7
Number of Residues	9
Details	binding site for residue LA F 203

Chain	Residue
B	HOH333
C	HOH320
C	HOH342
F	ASP121
F	HOH325
F	HOH335
F	HOH395
F	HOH408
F	HOH451

site_id	AG8
Number of Residues	8
Details	binding site for residue LA F 204

Chain	Residue
F	SER6
F	GLU11
F	HOH305
F	HOH351
F	HOH368
F	HOH412
F	HOH426
F	HOH441

site_id	AG9
Number of Residues	8
Details	binding site for residue LA F 205

Chain	Residue
A	LA206
A	HOH399
D	LA205
D	HOH454
F	GLU44
F	HOH304
F	HOH356
F	HOH429

site_id	AH1
Number of Residues	6
Details	binding site for residue LA F 206

Chain	Residue
D	ASP58
D	HOH379
D	HOH387
D	HOH394
D	HOH455
F	HOH425

site_id	AH2
Number of Residues	5
Details	binding site for residue LA F 207

Chain	Residue
F	GLU85
F	HOH354
F	HOH393
F	HOH420
F	HOH457

site_id	AH3
Number of Residues	4
Details	binding site for residue LA F 208

Chain	Residue
F	ASP58
F	LA210
F	HOH410
F	HOH415

site_id	AH4
Number of Residues	2
Details	binding site for residue LA F 209

Chain	Residue
F	ASP111
F	HOH423

site_id	AH5
Number of Residues	3
Details	binding site for residue LA F 210

Chain	Residue
B	HOH419
F	LA208
F	HOH442

Functional Information from PROSITE/UniProt

site_id	PS00818
Number of Residues	17
Details	DPS_1 Dps protein family signature 1. HWyMrGhnfftLHekmD

Chain	Residue	Details
E	HIS31-ASP47
A	HIS31-ASP47

site_id	PS00819
Number of Residues	15
Details	DPS_2 Dps protein family signature 2. MDeVAERllaIGgsP

Chain	Residue	Details
E	MET57-PRO71
A	MET57-PRO71

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:10625425

Chain	Residue	Details
E	HIS31
B	HIS31
C	HIS31
D	HIS31
F	HIS31

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: in other chain => ECO:0000269\|PubMed:10625425

Chain	Residue	Details
E	ASP58
B	ASP58
C	ASP58
D	ASP58
F	ASP58

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000305\|PubMed:10625425

Chain	Residue	Details
E	GLU62
B	GLU62
C	GLU62
D	GLU62
F	GLU62

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