Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3GSD

2.05 Angstrom structure of a divalent-cation tolerance protein (CutA) from Yersinia pestis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005507	molecular_function	copper ion binding
A	0005737	cellular_component	cytoplasm
A	0010038	biological_process	response to metal ion
A	0046872	molecular_function	metal ion binding
B	0005507	molecular_function	copper ion binding
B	0005737	cellular_component	cytoplasm
B	0010038	biological_process	response to metal ion
B	0046872	molecular_function	metal ion binding
C	0005507	molecular_function	copper ion binding
C	0005737	cellular_component	cytoplasm
C	0010038	biological_process	response to metal ion
C	0046872	molecular_function	metal ion binding
D	0005507	molecular_function	copper ion binding
D	0005737	cellular_component	cytoplasm
D	0010038	biological_process	response to metal ion
D	0046872	molecular_function	metal ion binding
E	0005507	molecular_function	copper ion binding
E	0005737	cellular_component	cytoplasm
E	0010038	biological_process	response to metal ion
E	0046872	molecular_function	metal ion binding
F	0005507	molecular_function	copper ion binding
F	0005737	cellular_component	cytoplasm
F	0010038	biological_process	response to metal ion
F	0046872	molecular_function	metal ion binding
G	0005507	molecular_function	copper ion binding
G	0005737	cellular_component	cytoplasm
G	0010038	biological_process	response to metal ion
G	0046872	molecular_function	metal ion binding
H	0005507	molecular_function	copper ion binding
H	0005737	cellular_component	cytoplasm
H	0010038	biological_process	response to metal ion
H	0046872	molecular_function	metal ion binding
I	0005507	molecular_function	copper ion binding
I	0005737	cellular_component	cytoplasm
I	0010038	biological_process	response to metal ion
I	0046872	molecular_function	metal ion binding
J	0005507	molecular_function	copper ion binding
J	0005737	cellular_component	cytoplasm
J	0010038	biological_process	response to metal ion
J	0046872	molecular_function	metal ion binding
K	0005507	molecular_function	copper ion binding
K	0005737	cellular_component	cytoplasm
K	0010038	biological_process	response to metal ion
K	0046872	molecular_function	metal ion binding
L	0005507	molecular_function	copper ion binding
L	0005737	cellular_component	cytoplasm
L	0010038	biological_process	response to metal ion
L	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA D 120

Chain	Residue
D	GLN32
F	HOH127
G	GLN32
G	NA120
I	HOH133
I	HOH143

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA I 120

Chain	Residue
I	HOH140
I	HOH141
J	GLN32
I	GLN32
I	NA122
I	HOH135

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA C 120

Chain	Residue
C	GLN32
E	HOH125
F	HOH203
I	HOH137
L	GLN32
L	NA120

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA F 120

Chain	Residue
F	GLN32
F	NA122
F	HOH184
H	GLN32
I	HOH128
I	HOH142

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 120

Chain	Residue
A	GLN32
A	NA122
E	HOH129
I	HOH126
I	HOH139
K	GLN32

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NA F 121

Chain	Residue
A	HOH249
A	HOH491
E	HOH128
E	HOH147
F	HOH446
F	HOH959
K	NA120

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NA K 120

Chain	Residue
A	HOH491
E	HOH128
F	NA121
F	HOH178
K	HOH250
K	HOH960
K	HOH961

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NA L 120

Chain	Residue
C	GLN32
C	NA120
C	HOH653
C	HOH655
C	HOH656
F	HOH131
L	GLN32

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NA I 121

Chain	Residue
B	NA120
B	HOH254
E	HOH161
I	HOH252
I	HOH542
J	HOH435
J	HOH498

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NA I 122

Chain	Residue
I	GLN32
I	NA120
I	HOH819
I	HOH821
J	GLN32
J	HOH329
J	HOH820

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NA E 120

Chain	Residue
B	GLN32
B	NA121
B	HOH473
B	HOH610
E	GLN32
E	HOH609
E	HOH1105

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NA B 120

Chain	Residue
B	HOH974
B	HOH975
F	HOH175
I	NA121
I	HOH542
J	HOH357
J	HOH435

site_id	BC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NA G 120

Chain	Residue
D	GLN32
D	NA120
D	HOH530
D	HOH675
G	GLN32
G	HOH770
G	HOH809

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA L 121

Chain	Residue
C	HOH258
C	HOH334
L	NA122
L	HOH925
L	HOH926
L	HOH1108

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 121

Chain	Residue
A	HOH373
A	HOH564
B	HOH417
B	HOH481
C	HOH206
C	HOH325

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NA F 122

Chain	Residue
F	NA120
F	HOH318
F	HOH507
F	HOH756
H	GLN32
H	HOH802
F	GLN32

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NA A 122

Chain	Residue
A	GLN32
A	NA120
A	HOH401
A	HOH521
A	HOH1114
K	GLN32
K	HOH888

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA B 121

Chain	Residue
B	GLN32
E	GLN32
E	NA120
E	HOH159
I	HOH129
I	HOH130

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA D 121

Chain	Residue
D	HOH227
E	HOH123
E	HOH146
E	HOH224
F	HOH136
F	HOH229

site_id	CC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA G 121

Chain	Residue
E	HOH141
E	HOH143
E	HOH144
G	HOH439
H	HOH346
I	HOH419

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA J 120

Chain	Residue
E	HOH148
E	HOH160
F	HOH142
J	HOH290
K	HOH337
L	HOH414

site_id	CC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NA L 122

Chain	Residue
C	HOH334
C	HOH338
L	NA121
L	HOH242
L	HOH470
L	HOH926
L	HOH1111

site_id	CC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG A 123

Chain	Residue
A	TYR67
A	HOH1010

site_id	CC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG B 122

Chain	Residue
B	TYR67
B	HOH1012
B	HOH1185
B	HOH1210

site_id	CC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG C 121

Chain	Residue
C	GLY52
C	TYR67
C	HOH650
C	HOH1147

site_id	CC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG D 122

Chain	Residue
D	TYR67
D	HOH976
D	HOH1233

site_id	CC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG E 121

Chain	Residue
E	TYR67
E	HOH973

site_id	DC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG F 123

Chain	Residue
F	TYR67
F	HOH1006
F	HOH1200
F	HOH1234

site_id	DC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG G 122

Chain	Residue
G	GLY52
G	TYR67
G	HOH992
G	HOH1224
G	HOH1235

site_id	DC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG H 120

Chain	Residue
H	GLY52
H	TYR67
H	HOH1142
H	HOH1230
H	HOH1236

site_id	DC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG I 123

Chain	Residue
I	TYR67
I	HOH1007

site_id	DC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG J 121

Chain	Residue
J	GLY52
J	TYR67
J	HOH1000
J	HOH1182
J	HOH1237

site_id	DC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG K 121

Chain	Residue
K	TYR67
K	HOH883

site_id	DC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG L 123

Chain	Residue
L	GLY52
L	TYR67
L	HOH1222

site_id	DC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO F 124

Chain	Residue
E	TRP113
F	TRP59
F	GLU60
F	HOH477

site_id	DC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO C 122

Chain	Residue
B	TRP113
C	TYR58
C	TRP59
C	GLU60
C	HOH406

site_id	EC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO H 121

Chain	Residue
G	TRP113
H	TYR58
H	TRP59
H	GLU60
H	HOH418

site_id	EC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE EPE A 124

Chain	Residue
A	THR24
A	TYR57
A	TRP59
A	GLU68
A	TYR93
A	GLN94
A	THR95
A	HOH478
A	HOH947
A	HOH948

site_id	EC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EPE B 123

Chain	Residue
B	THR24
B	TYR57
B	TRP59
B	GLU68
B	TYR93
B	GLN94
B	THR95
B	HOH543
B	HOH552

site_id	EC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE EPE C 123

Chain	Residue
C	THR24
C	TYR57
C	TRP59
C	GLU68
C	TYR93
C	GLN94
C	THR95
C	HOH375
C	HOH484
C	HOH1028

site_id	EC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE EPE D 123

Chain	Residue
D	THR24
D	TYR57
D	TRP59
D	GLU68
D	TYR93
D	GLN94
D	THR95
D	HOH231
D	HOH678
D	HOH700

site_id	EC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE EPE E 122

Chain	Residue
E	THR24
E	TYR57
E	TRP59
E	GLU68
E	TYR93
E	GLN94
E	THR95
E	HOH440
E	HOH464
E	HOH741

site_id	EC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE EPE F 125

Chain	Residue
F	THR24
F	TYR57
F	TRP59
F	GLU68
F	TYR93
F	GLN94
F	THR95
F	HOH395
F	HOH746
F	HOH764

site_id	EC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE EPE G 123

Chain	Residue
G	THR24
G	TYR57
G	TRP59
G	GLU68
G	TYR93
G	GLN94
G	THR95
G	HOH789
G	HOH790
G	HOH791
G	HOH949

site_id	EC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE EPE H 122

Chain	Residue
H	THR24
H	TYR57
H	TRP59
H	GLU68
H	TYR93
H	GLN94
H	THR95
H	HOH234
H	HOH359
H	HOH950

site_id	FC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE EPE I 124

Chain	Residue
I	THR24
I	TYR57
I	TRP59
I	GLU68
I	TYR93
I	GLN94
I	THR95
I	HOH381
I	HOH838
I	HOH951

site_id	FC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE EPE J 122

Chain	Residue
J	THR24
J	TYR57
J	TRP59
J	GLU68
J	TYR93
J	GLN94
J	THR95
J	HOH282
J	HOH868
J	HOH952

site_id	FC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE EPE K 122

Chain	Residue
K	THR24
K	TYR57
K	TRP59
K	GLU68
K	TYR93
K	GLN94
K	THR95
K	HOH898
K	HOH899
K	HOH953

site_id	FC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE EPE L 124

Chain	Residue
K	TYR110
K	TRP113
K	HOH214
L	TYR57
L	TRP59
L	TYR93
L	GLN94
L	THR95
L	HOH270
L	HOH393
L	HOH942

site_id	FC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EPE L 125

Chain	Residue
E	THR77
E	ASP78
J	GLN81
L	ASP105
L	GLY106
L	ASP107
L	LYS108
L	HOH965

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_01160

Chain	Residue	Details
A	CYS23
A	HIS90
A	HIS91
B	CYS23
B	HIS90
B	HIS91
C	CYS23
C	HIS90
C	HIS91
D	CYS23
D	HIS90
D	HIS91
E	CYS23
E	HIS90
E	HIS91
F	CYS23
F	HIS90
F	HIS91
G	CYS23
G	HIS91
H	CYS23
H	HIS90
H	HIS91
I	CYS23
I	HIS90
I	HIS91
J	CYS23
J	HIS90
J	HIS91
K	CYS23
K	HIS90
K	HIS91
L	CYS23
L	HIS90
L	HIS91
G	HIS90

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