Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5EY8

Structure of FadD32 from Mycobacterium smegmatis complexed to AMPC20

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006631	biological_process	fatty acid metabolic process
A	0006633	biological_process	fatty acid biosynthetic process
A	0008610	biological_process	lipid biosynthetic process
A	0008922	molecular_function	long-chain fatty acid [acyl-carrier-protein] ligase activity
A	0016874	molecular_function	ligase activity
A	0070566	molecular_function	adenylyltransferase activity
B	0005524	molecular_function	ATP binding
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006631	biological_process	fatty acid metabolic process
B	0006633	biological_process	fatty acid biosynthetic process
B	0008610	biological_process	lipid biosynthetic process
B	0008922	molecular_function	long-chain fatty acid [acyl-carrier-protein] ligase activity
B	0016874	molecular_function	ligase activity
B	0070566	molecular_function	adenylyltransferase activity
C	0005524	molecular_function	ATP binding
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0006631	biological_process	fatty acid metabolic process
C	0006633	biological_process	fatty acid biosynthetic process
C	0008610	biological_process	lipid biosynthetic process
C	0008922	molecular_function	long-chain fatty acid [acyl-carrier-protein] ligase activity
C	0016874	molecular_function	ligase activity
C	0070566	molecular_function	adenylyltransferase activity
D	0005524	molecular_function	ATP binding
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0006631	biological_process	fatty acid metabolic process
D	0006633	biological_process	fatty acid biosynthetic process
D	0008610	biological_process	lipid biosynthetic process
D	0008922	molecular_function	long-chain fatty acid [acyl-carrier-protein] ligase activity
D	0016874	molecular_function	ligase activity
D	0070566	molecular_function	adenylyltransferase activity
E	0005524	molecular_function	ATP binding
E	0005829	cellular_component	cytosol
E	0005886	cellular_component	plasma membrane
E	0006631	biological_process	fatty acid metabolic process
E	0006633	biological_process	fatty acid biosynthetic process
E	0008610	biological_process	lipid biosynthetic process
E	0008922	molecular_function	long-chain fatty acid [acyl-carrier-protein] ligase activity
E	0016874	molecular_function	ligase activity
E	0070566	molecular_function	adenylyltransferase activity
F	0005524	molecular_function	ATP binding
F	0005829	cellular_component	cytosol
F	0005886	cellular_component	plasma membrane
F	0006631	biological_process	fatty acid metabolic process
F	0006633	biological_process	fatty acid biosynthetic process
F	0008610	biological_process	lipid biosynthetic process
F	0008922	molecular_function	long-chain fatty acid [acyl-carrier-protein] ligase activity
F	0016874	molecular_function	ligase activity
F	0070566	molecular_function	adenylyltransferase activity
G	0005524	molecular_function	ATP binding
G	0005829	cellular_component	cytosol
G	0005886	cellular_component	plasma membrane
G	0006631	biological_process	fatty acid metabolic process
G	0006633	biological_process	fatty acid biosynthetic process
G	0008610	biological_process	lipid biosynthetic process
G	0008922	molecular_function	long-chain fatty acid [acyl-carrier-protein] ligase activity
G	0016874	molecular_function	ligase activity
G	0070566	molecular_function	adenylyltransferase activity
H	0005524	molecular_function	ATP binding
H	0005829	cellular_component	cytosol
H	0005886	cellular_component	plasma membrane
H	0006631	biological_process	fatty acid metabolic process
H	0006633	biological_process	fatty acid biosynthetic process
H	0008610	biological_process	lipid biosynthetic process
H	0008922	molecular_function	long-chain fatty acid [acyl-carrier-protein] ligase activity
H	0016874	molecular_function	ligase activity
H	0070566	molecular_function	adenylyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	binding site for residue 5SV A 701

Chain	Residue
A	HIS231
A	TYR343
A	GLY344
A	LEU345
A	ALA346
A	LEU350
A	ASP469
A	ILE480
A	ARG483
A	ASP232
A	THR237
A	ILE278
A	LEU311
A	SER314
A	GLU315
A	PRO316
A	SER342

site_id	AC2
Number of Residues	13
Details	binding site for residue 5SV B 701

Chain	Residue
B	HIS231
B	ASP232
B	THR237
B	SER314
B	PRO316
B	SER342
B	TYR343
B	GLY344
B	LEU345
B	ALA346
B	LEU350
B	ASP469
B	ARG483

site_id	AC3
Number of Residues	16
Details	binding site for residue 5SV C 701

Chain	Residue
C	HIS231
C	ASP232
C	MET233
C	THR237
C	LEU240
C	LEU311
C	SER314
C	GLU315
C	PRO316
C	SER342
C	TYR343
C	GLY344
C	LEU345
C	LEU350
C	ASP469
C	ARG483

site_id	AC4
Number of Residues	15
Details	binding site for residue 5SV D 701

Chain	Residue
D	GLY223
D	HIS231
D	ASP232
D	LEU311
D	SER314
D	GLU315
D	PRO316
D	SER342
D	TYR343
D	GLY344
D	ALA346
D	LEU350
D	ASP469
D	ARG483
D	LYS601

site_id	AC5
Number of Residues	15
Details	binding site for residue 5SV E 701

Chain	Residue
E	VAL211
E	HIS231
E	ASP232
E	THR237
E	LEU311
E	SER314
E	GLU315
E	PRO316
E	SER342
E	TYR343
E	GLY344
E	LEU345
E	LEU350
E	ASP469
E	ARG483

site_id	AC6
Number of Residues	4
Details	binding site for residue GOL E 702

Chain	Residue
E	ALA386
E	VAL387
E	ALA388
E	TYR502

site_id	AC7
Number of Residues	13
Details	binding site for residue 5SV F 701

Chain	Residue
F	HIS231
F	ASP232
F	THR237
F	SER314
F	GLU315
F	PRO316
F	SER342
F	TYR343
F	GLY344
F	LEU345
F	LEU350
F	ASP469
F	ARG483

site_id	AC8
Number of Residues	2
Details	binding site for residue GOL F 702

Chain	Residue
F	ALA386
F	ALA388

site_id	AC9
Number of Residues	14
Details	binding site for residue 5SV G 701

Chain	Residue
G	SER314
G	PRO316
G	ILE317
G	SER342
G	TYR343
G	GLY344
G	LEU345
G	LEU350
G	ASP469
G	ARG483
G	HIS231
G	ASP232
G	MET233
G	LEU311

site_id	AD1
Number of Residues	14
Details	binding site for residue 5SV H 701

Chain	Residue
H	HIS231
H	ASP232
H	THR237
H	VAL280
H	LEU311
H	SER314
H	ILE317
H	SER342
H	TYR343
H	GLY344
H	LEU345
H	ALA346
H	ASP469
H	ILE480

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	40
Details	BINDING: BINDING => ECO:0000269\|PubMed:26628098, ECO:0007744\|PDB:5D6J

Chain	Residue	Details
B	ASP469
B	ARG483
C	THR187
C	SER342
C	ALA346
C	ASP469
C	ARG483
D	THR187
D	SER342
D	ALA346
D	ASP469
D	ARG483
E	THR187
E	SER342
E	ALA346
E	ASP469
E	ARG483
F	THR187
F	SER342
F	ALA346
F	ASP469
F	ARG483
G	THR187
G	SER342
G	ALA346
G	ASP469
G	ARG483
H	THR187
H	SER342
H	ALA346
H	ASP469
H	ARG483
A	THR187
A	SER342
A	ALA346
A	ASP469
A	ARG483
B	THR187
B	SER342
B	ALA346

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