Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5O8Q

Crystal structure of R. ruber ADH-A, mutant Y294F, W295A

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008270	molecular_function	zinc ion binding
A	0016491	molecular_function	oxidoreductase activity
B	0008270	molecular_function	zinc ion binding
B	0016491	molecular_function	oxidoreductase activity
C	0008270	molecular_function	zinc ion binding
C	0016491	molecular_function	oxidoreductase activity
D	0008270	molecular_function	zinc ion binding
D	0016491	molecular_function	oxidoreductase activity
E	0008270	molecular_function	zinc ion binding
E	0016491	molecular_function	oxidoreductase activity
F	0008270	molecular_function	zinc ion binding
F	0016491	molecular_function	oxidoreductase activity
G	0008270	molecular_function	zinc ion binding
G	0016491	molecular_function	oxidoreductase activity
H	0008270	molecular_function	zinc ion binding
H	0016491	molecular_function	oxidoreductase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue ZN A 501

Chain	Residue
A	CYS38
A	SER40
A	HIS62
A	ASP153
A	NAD503

site_id	AC2
Number of Residues	4
Details	binding site for residue ZN A 502

Chain	Residue
A	CYS92
A	CYS95
A	CYS98
A	CYS106

site_id	AC3
Number of Residues	27
Details	binding site for residue NAD A 503

Chain	Residue
A	HIS39
A	ASP153
A	THR157
A	VAL180
A	GLY181
A	GLY182
A	LEU183
A	ASP203
A	LEU204
A	ARG208
A	SER223
A	PHE246
A	VAL247
A	THR252
A	VAL269
A	GLY270
A	ILE271
A	PRO293
A	PHE294
A	ALA295
A	ARG340
A	ZN501
A	HOH610
A	HOH619
A	HOH626
A	HOH629
A	HOH646

site_id	AC4
Number of Residues	3
Details	binding site for residue ZN B 501

Chain	Residue
B	CYS38
B	HIS62
B	ASP153

site_id	AC5
Number of Residues	4
Details	binding site for residue ZN B 502

Chain	Residue
B	CYS92
B	CYS95
B	CYS98
B	CYS106

site_id	AC6
Number of Residues	29
Details	binding site for residue NAD B 503

Chain	Residue
B	HIS39
B	ASP153
B	THR157
B	VAL180
B	GLY181
B	GLY182
B	LEU183
B	ASP203
B	LEU204
B	ARG208
B	SER223
B	PHE246
B	VAL247
B	THR252
B	VAL269
B	GLY270
B	ILE271
B	PRO293
B	PHE294
B	ALA295
B	ARG340
B	HOH614
B	HOH621
B	HOH636
B	HOH643
B	HOH653
B	HOH658
B	HOH678
B	HOH689

site_id	AC7
Number of Residues	4
Details	binding site for residue ZN C 501

Chain	Residue
C	CYS38
C	HIS62
C	ASP153
C	NAD503

site_id	AC8
Number of Residues	4
Details	binding site for residue ZN C 502

Chain	Residue
C	CYS92
C	CYS95
C	CYS98
C	CYS106

site_id	AC9
Number of Residues	30
Details	binding site for residue NAD C 503

Chain	Residue
C	ALA295
C	ARG340
C	ZN501
C	HOH604
C	HOH613
C	HOH619
C	HOH623
C	HOH630
C	HOH662
C	HOH666
F	PHE281
C	HIS39
C	ASP153
C	THR157
C	VAL180
C	GLY181
C	GLY182
C	LEU183
C	ASP203
C	LEU204
C	ARG208
C	SER223
C	PHE246
C	VAL247
C	THR252
C	VAL269
C	GLY270
C	ILE271
C	PRO293
C	PHE294

site_id	AD1
Number of Residues	5
Details	binding site for residue ZN D 501

Chain	Residue
D	CYS38
D	HIS62
D	ASP153
D	NAD503
D	HOH697

site_id	AD2
Number of Residues	4
Details	binding site for residue ZN D 502

Chain	Residue
D	CYS92
D	CYS95
D	CYS98
D	CYS106

site_id	AD3
Number of Residues	31
Details	binding site for residue NAD D 503

Chain	Residue
D	HIS39
D	ASP153
D	THR157
D	GLY179
D	VAL180
D	GLY181
D	GLY182
D	LEU183
D	ASP203
D	LEU204
D	ARG208
D	SER223
D	PHE246
D	VAL247
D	THR252
D	VAL269
D	GLY270
D	ILE271
D	PRO293
D	PHE294
D	ALA295
D	ARG340
D	ZN501
D	HOH604
D	HOH622
D	HOH630
D	HOH640
D	HOH649
D	HOH651
D	HOH690
D	HOH695

site_id	AD4
Number of Residues	4
Details	binding site for residue ZN E 501

Chain	Residue
E	CYS38
E	HIS62
E	ASP153
E	NAD503

site_id	AD5
Number of Residues	4
Details	binding site for residue ZN E 502

Chain	Residue
E	CYS92
E	CYS95
E	CYS98
E	CYS106

site_id	AD6
Number of Residues	30
Details	binding site for residue NAD E 503

Chain	Residue
E	HIS39
E	ASP153
E	THR157
E	VAL180
E	GLY181
E	GLY182
E	LEU183
E	ASP203
E	LEU204
E	ARG208
E	SER223
E	PHE246
E	VAL247
E	THR252
E	VAL269
E	GLY270
E	ILE271
E	PRO293
E	PHE294
E	ALA295
E	ARG340
E	ZN501
E	HOH608
E	HOH611
E	HOH614
E	HOH623
E	HOH627
E	HOH636
E	HOH653
E	HOH660

site_id	AD7
Number of Residues	4
Details	binding site for residue ZN F 501

Chain	Residue
F	CYS38
F	HIS62
F	ASP153
F	NAD503

site_id	AD8
Number of Residues	4
Details	binding site for residue ZN F 502

Chain	Residue
F	CYS92
F	CYS95
F	CYS98
F	CYS106

site_id	AD9
Number of Residues	28
Details	binding site for residue NAD F 503

Chain	Residue
F	HIS39
F	ASP153
F	THR157
F	VAL180
F	GLY181
F	GLY182
F	LEU183
F	ASP203
F	LEU204
F	ARG208
F	SER223
F	PHE246
F	VAL247
F	THR252
F	VAL269
F	ILE271
F	PRO293
F	PHE294
F	ALA295
F	ARG340
F	ZN501
F	HOH608
F	HOH614
F	HOH615
F	HOH641
F	HOH646
F	HOH648
F	HOH676

site_id	AE1
Number of Residues	5
Details	binding site for residue ZN G 501

Chain	Residue
G	CYS38
G	HIS62
G	ASP153
G	NAD503
G	HOH659

site_id	AE2
Number of Residues	4
Details	binding site for residue ZN G 502

Chain	Residue
G	CYS92
G	CYS95
G	CYS98
G	CYS106

site_id	AE3
Number of Residues	28
Details	binding site for residue NAD G 503

Chain	Residue
D	PHE281
G	HIS39
G	ASP153
G	THR157
G	VAL180
G	GLY181
G	GLY182
G	LEU183
G	ASP203
G	LEU204
G	ARG208
G	SER223
G	PHE246
G	VAL247
G	THR252
G	VAL269
G	GLY270
G	ILE271
G	PRO293
G	PHE294
G	ALA295
G	ARG340
G	ZN501
G	HOH605
G	HOH609
G	HOH618
G	HOH634
G	HOH642

site_id	AE4
Number of Residues	3
Details	binding site for residue ZN H 501

Chain	Residue
H	CYS38
H	ASP153
H	NAD503

site_id	AE5
Number of Residues	4
Details	binding site for residue ZN H 502

Chain	Residue
H	CYS92
H	CYS95
H	CYS98
H	CYS106

site_id	AE6
Number of Residues	23
Details	binding site for residue NAD H 503

Chain	Residue
H	HIS39
H	ASP153
H	THR157
H	VAL180
H	GLY181
H	GLY182
H	LEU183
H	ASP203
H	LEU204
H	ASP205
H	ARG208
H	SER223
H	PHE246
H	VAL247
H	VAL269
H	ILE271
H	PRO293
H	PHE294
H	ALA295
H	ARG340
H	ZN501
H	HOH602
H	HOH646

Functional Information from PROSITE/UniProt

site_id	PS00059
Number of Residues	15
Details	ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEgVGTvaelGegV

Chain	Residue	Details
A	GLY61-VAL75

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