Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7DO6

Crystal structure of Azotobacter vinelandii L-rhamnose 1-dehydrogenase(NADP bound-form)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0006633	biological_process	fatty acid biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0019301	biological_process	rhamnose catabolic process
A	0019318	biological_process	hexose metabolic process
A	0048038	molecular_function	quinone binding
B	0000166	molecular_function	nucleotide binding
B	0006633	biological_process	fatty acid biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0019301	biological_process	rhamnose catabolic process
B	0019318	biological_process	hexose metabolic process
B	0048038	molecular_function	quinone binding
C	0000166	molecular_function	nucleotide binding
C	0006633	biological_process	fatty acid biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
C	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C	0019301	biological_process	rhamnose catabolic process
C	0019318	biological_process	hexose metabolic process
C	0048038	molecular_function	quinone binding
D	0000166	molecular_function	nucleotide binding
D	0006633	biological_process	fatty acid biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
D	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D	0019301	biological_process	rhamnose catabolic process
D	0019318	biological_process	hexose metabolic process
D	0048038	molecular_function	quinone binding
E	0000166	molecular_function	nucleotide binding
E	0006633	biological_process	fatty acid biosynthetic process
E	0016491	molecular_function	oxidoreductase activity
E	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
E	0019301	biological_process	rhamnose catabolic process
E	0019318	biological_process	hexose metabolic process
E	0048038	molecular_function	quinone binding
F	0000166	molecular_function	nucleotide binding
F	0006633	biological_process	fatty acid biosynthetic process
F	0016491	molecular_function	oxidoreductase activity
F	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
F	0019301	biological_process	rhamnose catabolic process
F	0019318	biological_process	hexose metabolic process
F	0048038	molecular_function	quinone binding
G	0000166	molecular_function	nucleotide binding
G	0006633	biological_process	fatty acid biosynthetic process
G	0016491	molecular_function	oxidoreductase activity
G	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
G	0019301	biological_process	rhamnose catabolic process
G	0019318	biological_process	hexose metabolic process
G	0048038	molecular_function	quinone binding
H	0000166	molecular_function	nucleotide binding
H	0006633	biological_process	fatty acid biosynthetic process
H	0016491	molecular_function	oxidoreductase activity
H	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
H	0019301	biological_process	rhamnose catabolic process
H	0019318	biological_process	hexose metabolic process
H	0048038	molecular_function	quinone binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	binding site for residue NAP A 301

Chain	Residue
A	GLY12
A	ALA67
A	ASN93
A	ALA94
A	GLY95
A	ILE96
A	THR116
A	SER145
A	SER146
A	TYR159
A	LYS163
A	SER14
A	GLY190
A	ILE192
A	HOH406
A	HOH416
A	HOH437
A	ARG15
A	GLY16
A	ILE17
A	HIS36
A	SER37
A	GLY42
A	ASP66

site_id	AC2
Number of Residues	24
Details	binding site for residue NAP B 301

Chain	Residue
B	GLY12
B	SER14
B	ARG15
B	GLY16
B	ILE17
B	HIS36
B	SER37
B	GLY42
B	ASP66
B	ALA67
B	ASN93
B	ALA94
B	GLY95
B	ILE96
B	THR116
B	VAL144
B	SER145
B	SER146
B	TYR159
B	LYS163
B	PRO189
B	GLY190
B	ILE192
B	THR194

site_id	AC3
Number of Residues	29
Details	binding site for residue NAP C 301

Chain	Residue
C	GLY12
C	SER14
C	ARG15
C	GLY16
C	ILE17
C	SER37
C	GLY42
C	ALA65
C	ASP66
C	ALA67
C	ALA68
C	ASN93
C	ALA94
C	GLY95
C	ILE96
C	VAL144
C	SER145
C	SER146
C	TYR159
C	LYS163
C	PRO189
C	GLY190
C	ILE192
C	THR194
C	ASP195
C	ILE196
C	ASN197
C	HOH402
C	HOH412

site_id	AC4
Number of Residues	25
Details	binding site for residue NAP D 301

Chain	Residue
D	ILE192
D	THR194
D	HOH430
D	GLY12
D	ALA13
D	SER14
D	ARG15
D	GLY16
D	ILE17
D	HIS36
D	SER37
D	GLY42
D	ALA65
D	ASP66
D	ALA67
D	ASN93
D	ALA94
D	GLY95
D	VAL144
D	SER145
D	SER146
D	TYR159
D	LYS163
D	PRO189
D	GLY190

site_id	AC5
Number of Residues	26
Details	binding site for residue NAP E 301

Chain	Residue
E	GLY12
E	SER14
E	ARG15
E	GLY16
E	ILE17
E	HIS36
E	SER37
E	GLY42
E	ALA65
E	ASP66
E	ALA67
E	ASN93
E	ALA94
E	GLY95
E	ILE96
E	VAL144
E	SER145
E	SER146
E	TYR159
E	LYS163
E	PRO189
E	GLY190
E	ILE192
E	HOH429
E	HOH432
E	HOH437

site_id	AC6
Number of Residues	26
Details	binding site for residue NAP F 301

Chain	Residue
F	GLY12
F	ALA13
F	SER14
F	ARG15
F	GLY16
F	ILE17
F	HIS36
F	SER37
F	GLY42
F	ALA65
F	ASP66
F	ALA67
F	ASN93
F	ALA94
F	GLY95
F	ILE96
F	VAL144
F	SER145
F	SER146
F	TYR159
F	LYS163
F	PRO189
F	GLY190
F	ILE192
F	HOH401
F	HOH406

site_id	AC7
Number of Residues	21
Details	binding site for residue NAP G 301

Chain	Residue
G	GLY12
G	SER14
G	ILE17
G	HIS36
G	SER37
G	GLY42
G	ASP66
G	ALA67
G	ASN93
G	GLY95
G	ILE96
G	VAL144
G	SER145
G	SER146
G	TYR159
G	LYS163
G	PRO189
G	GLY190
G	ILE192
G	THR194
G	HOH426

site_id	AC8
Number of Residues	26
Details	binding site for residue NAP H 301

Chain	Residue
H	GLY12
H	SER14
H	ARG15
H	GLY16
H	ILE17
H	HIS36
H	SER37
H	SER39
H	GLY42
H	ASP66
H	ALA67
H	ASN93
H	ALA94
H	GLY95
H	ILE96
H	VAL144
H	SER145
H	SER146
H	TYR159
H	LYS163
H	PRO189
H	GLY190
H	ILE192
H	HOH401
H	HOH412
H	HOH430

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"O93868","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"O93868","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Active site: {"description":"Lowers pKa of active site Tyr","evidences":[{"source":"UniProtKB","id":"O93868","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	80
Details	Binding site: {"evidences":[{"source":"PubMed","id":"33482017","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7B81","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7DO6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7DO7","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"33482017","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DO6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	34
Details	Binding site: {"evidences":[{"source":"PubMed","id":"33482017","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DO7","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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