Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5YCR

X-Ray Structure of Enoyl-Acyl Carrier Protein Reductase from Bacillus Anthracis with NAD+

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
A	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
A	0006633	biological_process	fatty acid biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0030497	biological_process	fatty acid elongation
A	0036094	molecular_function	small molecule binding
A	0042802	molecular_function	identical protein binding
A	0070401	molecular_function	NADP+ binding
A	0141148	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADPH) activity
A	1902494	cellular_component	catalytic complex
B	0000166	molecular_function	nucleotide binding
B	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
B	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
B	0006633	biological_process	fatty acid biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0030497	biological_process	fatty acid elongation
B	0036094	molecular_function	small molecule binding
B	0042802	molecular_function	identical protein binding
B	0070401	molecular_function	NADP+ binding
B	0141148	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADPH) activity
B	1902494	cellular_component	catalytic complex
C	0000166	molecular_function	nucleotide binding
C	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
C	0006629	biological_process	lipid metabolic process
C	0006631	biological_process	fatty acid metabolic process
C	0006633	biological_process	fatty acid biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
C	0030497	biological_process	fatty acid elongation
C	0036094	molecular_function	small molecule binding
C	0042802	molecular_function	identical protein binding
C	0070401	molecular_function	NADP+ binding
C	0141148	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADPH) activity
C	1902494	cellular_component	catalytic complex
D	0000166	molecular_function	nucleotide binding
D	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
D	0006629	biological_process	lipid metabolic process
D	0006631	biological_process	fatty acid metabolic process
D	0006633	biological_process	fatty acid biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
D	0030497	biological_process	fatty acid elongation
D	0036094	molecular_function	small molecule binding
D	0042802	molecular_function	identical protein binding
D	0070401	molecular_function	NADP+ binding
D	0141148	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADPH) activity
D	1902494	cellular_component	catalytic complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	25
Details	binding site for residue NAD A 301

Chain	Residue
A	GLY13
A	VAL67
A	CYS93
A	ILE94
A	ALA95
A	LEU145
A	THR146
A	LYS164
A	ALA190
A	LEU196
A	HOH403
A	VAL14
A	HOH404
A	HOH437
A	HOH450
A	HOH471
A	HOH474
A	HOH526
A	ALA15
A	SER19
A	ILE20
A	ALA40
A	LEU44
A	CYS65
A	ASP66

site_id	AC2
Number of Residues	5
Details	binding site for residue SO4 A 302

Chain	Residue
A	ARG26
A	ASN30
A	HOH524
D	ARG26
D	HOH438

site_id	AC3
Number of Residues	4
Details	binding site for residue SO4 A 303

Chain	Residue
A	ARG130
A	LYS134
A	HOH402
A	HOH449

site_id	AC4
Number of Residues	5
Details	binding site for residue SO4 A 304

Chain	Residue
A	ARG130
A	HOH405
A	HOH513
A	HOH517
C	ASP108

site_id	AC5
Number of Residues	6
Details	binding site for residue SO4 A 305

Chain	Residue
A	HIS247
A	HIS253
A	HOH502
A	HOH519
A	HOH521
B	GLU244

site_id	AC6
Number of Residues	5
Details	binding site for residue SO4 A 306

Chain	Residue
A	ARG239
A	HOH500
B	THR222
B	GLU224
B	HOH428

site_id	AC7
Number of Residues	26
Details	binding site for residue NAD B 301

Chain	Residue
B	GLY13
B	VAL14
B	ALA15
B	SER19
B	ILE20
B	ALA40
B	LEU44
B	CYS65
B	ASP66
B	VAL67
B	CYS93
B	ILE94
B	ALA95
B	LEU145
B	THR146
B	TYR147
B	LYS164
B	ALA190
B	LEU196
B	HOH401
B	HOH456
B	HOH464
B	HOH476
B	HOH489
B	HOH496
B	HOH519

site_id	AC8
Number of Residues	3
Details	binding site for residue SO4 B 302

Chain	Residue
B	ARG130
B	LYS134
B	HOH467

site_id	AC9
Number of Residues	4
Details	binding site for residue SO4 B 303

Chain	Residue
B	ARG130
B	HOH402
B	HOH415
D	ASP108

site_id	AD1
Number of Residues	5
Details	binding site for residue SO4 B 304

Chain	Residue
A	THR222
A	GLU224
A	HOH416
B	ARG239
D	MET1

site_id	AD2
Number of Residues	5
Details	binding site for residue SO4 B 305

Chain	Residue
A	GLU244
B	HIS253
B	HOH412
B	HOH442
B	HOH511

site_id	AD3
Number of Residues	27
Details	binding site for residue NAD C 301

Chain	Residue
C	LEU44
C	CYS65
C	ASP66
C	VAL67
C	THR68
C	CYS93
C	ILE94
C	ALA95
C	LEU145
C	THR146
C	TYR147
C	LYS164
C	ALA190
C	HOH401
C	HOH408
C	HOH411
C	HOH413
C	HOH447
C	HOH482
C	HOH486
C	HOH521
C	GLY13
C	VAL14
C	ALA15
C	SER19
C	ILE20
C	ALA40

site_id	AD4
Number of Residues	3
Details	binding site for residue SO4 C 302

Chain	Residue
C	ARG130
C	LYS134
C	HOH426

site_id	AD5
Number of Residues	6
Details	binding site for residue SO4 C 303

Chain	Residue
C	HIS253
C	HOH403
C	HOH422
C	HOH473
D	LYS172
D	GLU244

site_id	AD6
Number of Residues	3
Details	binding site for residue SO4 C 304

Chain	Residue
C	THR222
C	GLU224
D	ARG239

site_id	AD7
Number of Residues	3
Details	binding site for residue SO4 C 305

Chain	Residue
C	ARG239
D	THR222
D	GLU224

site_id	AD8
Number of Residues	22
Details	binding site for residue NAD D 301

Chain	Residue
D	GLY13
D	VAL14
D	ALA15
D	SER19
D	ILE20
D	ALA40
D	LEU44
D	CYS65
D	ASP66
D	VAL67
D	CYS93
D	ILE94
D	ALA95
D	LEU145
D	THR146
D	TYR147
D	LYS164
D	ALA190
D	HOH431
D	HOH435
D	HOH451
D	HOH466

site_id	AD9
Number of Residues	3
Details	binding site for residue SO4 D 302

Chain	Residue
D	ARG130
D	LYS134
D	HOH454

site_id	AE1
Number of Residues	4
Details	binding site for residue SO4 D 303

Chain	Residue
B	SER110
D	ARG130
D	HOH407
D	HOH426

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20800575","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Site: {"description":"Involved in acyl-ACP binding","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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