Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6JQN

Structure of PaaZ, a bifunctional enzyme in complex with NADP+ and OCoA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004300	molecular_function	enoyl-CoA hydratase activity
A	0010124	biological_process	phenylacetate catabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0016726	molecular_function	oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor
A	0016803	molecular_function	ether hydrolase activity
A	0016823	molecular_function	hydrolase activity, acting on carbon-carbon bonds, in ketonic substances
A	0042802	molecular_function	identical protein binding
B	0004300	molecular_function	enoyl-CoA hydratase activity
B	0010124	biological_process	phenylacetate catabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0016726	molecular_function	oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor
B	0016803	molecular_function	ether hydrolase activity
B	0016823	molecular_function	hydrolase activity, acting on carbon-carbon bonds, in ketonic substances
B	0042802	molecular_function	identical protein binding
C	0004300	molecular_function	enoyl-CoA hydratase activity
C	0010124	biological_process	phenylacetate catabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0016726	molecular_function	oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor
C	0016803	molecular_function	ether hydrolase activity
C	0016823	molecular_function	hydrolase activity, acting on carbon-carbon bonds, in ketonic substances
C	0042802	molecular_function	identical protein binding
D	0004300	molecular_function	enoyl-CoA hydratase activity
D	0010124	biological_process	phenylacetate catabolic process
D	0016491	molecular_function	oxidoreductase activity
D	0016726	molecular_function	oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor
D	0016803	molecular_function	ether hydrolase activity
D	0016823	molecular_function	hydrolase activity, acting on carbon-carbon bonds, in ketonic substances
D	0042802	molecular_function	identical protein binding
E	0004300	molecular_function	enoyl-CoA hydratase activity
E	0010124	biological_process	phenylacetate catabolic process
E	0016491	molecular_function	oxidoreductase activity
E	0016726	molecular_function	oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor
E	0016803	molecular_function	ether hydrolase activity
E	0016823	molecular_function	hydrolase activity, acting on carbon-carbon bonds, in ketonic substances
E	0042802	molecular_function	identical protein binding
F	0004300	molecular_function	enoyl-CoA hydratase activity
F	0010124	biological_process	phenylacetate catabolic process
F	0016491	molecular_function	oxidoreductase activity
F	0016726	molecular_function	oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor
F	0016803	molecular_function	ether hydrolase activity
F	0016823	molecular_function	hydrolase activity, acting on carbon-carbon bonds, in ketonic substances
F	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	23
Details	binding site for residue NAP A 801

Chain	Residue
A	ARG20
A	THR184
A	PHE230
A	THR231
A	GLY232
A	SER233
A	THR236
A	LEU240
A	GLU256
A	ALA257
A	ASP258
A	ILE154
A	CYS295
A	GLU395
A	PHE397
A	HIS472
A	ASN155
A	ALA156
A	PHE157
A	ASN158
A	LYS181
A	PRO182
A	ALA183

site_id	AC2
Number of Residues	12
Details	binding site for residue CO8 A 802

Chain	Residue
A	PHE563
A	HIS566
A	PHE577
A	VAL582
A	GLY584
A	ARG613
A	PHE614
A	ILE615
B	ARG116
B	ASN606
B	TYR607
B	LYS636

site_id	AC3
Number of Residues	23
Details	binding site for residue NAP B 801

Chain	Residue
B	ARG20
B	ILE154
B	ASN155
B	ALA156
B	PHE157
B	ASN158
B	LYS181
B	ALA183
B	THR184
B	PHE230
B	THR231
B	GLY232
B	SER233
B	THR236
B	LEU240
B	GLU256
B	ALA257
B	ASP258
B	CYS295
B	GLU395
B	PHE397
B	LEU423
B	HIS472

site_id	AC4
Number of Residues	9
Details	binding site for residue CO8 B 802

Chain	Residue
A	ALA605
A	ASN606
A	TYR607
A	LYS636
B	PHE563
B	HIS566
B	PHE614
B	ILE615
B	PRO617

site_id	AC5
Number of Residues	23
Details	binding site for residue NAP C 801

Chain	Residue
C	ARG20
C	ILE154
C	ASN155
C	ALA156
C	PHE157
C	ASN158
C	LYS181
C	ALA183
C	THR184
C	PHE230
C	THR231
C	GLY232
C	SER233
C	THR236
C	LEU240
C	GLU256
C	ALA257
C	ASP258
C	CYS295
C	GLU395
C	PHE397
C	LEU423
C	HIS472

site_id	AC6
Number of Residues	13
Details	binding site for residue CO8 C 802

Chain	Residue
D	ALA605
D	ASN606
D	TYR607
D	LYS636
C	PHE563
C	HIS566
C	PHE577
C	VAL582
C	GLY584
C	PHE614
C	ILE615
C	PRO617
C	LEU665

site_id	AC7
Number of Residues	23
Details	binding site for residue NAP D 801

Chain	Residue
D	ARG20
D	ILE154
D	ASN155
D	ALA156
D	PHE157
D	ASN158
D	LYS181
D	ALA183
D	THR184
D	PHE230
D	THR231
D	GLY232
D	SER233
D	THR236
D	LEU240
D	GLU256
D	ALA257
D	ASP258
D	CYS295
D	GLU395
D	PHE397
D	LEU423
D	HIS472

site_id	AC8
Number of Residues	11
Details	binding site for residue CO8 D 802

Chain	Residue
C	ASN606
C	TYR607
C	LYS636
D	PHE563
D	HIS566
D	PHE577
D	VAL582
D	ARG613
D	PHE614
D	ILE615
D	LEU665

site_id	AC9
Number of Residues	22
Details	binding site for residue NAP E 801

Chain	Residue
E	ARG20
E	ASN155
E	ALA156
E	PHE157
E	ASN158
E	LYS181
E	ALA183
E	THR184
E	PHE230
E	THR231
E	GLY232
E	SER233
E	THR236
E	LEU240
E	GLU256
E	ALA257
E	ASP258
E	CYS295
E	GLU395
E	PHE397
E	LEU423
E	HIS472

site_id	AD1
Number of Residues	10
Details	binding site for residue CO8 E 802

Chain	Residue
E	PHE563
E	HIS566
E	PHE577
E	PHE614
E	ILE615
F	VAL596
F	ALA605
F	ASN606
F	TYR607
F	LYS636

site_id	AD2
Number of Residues	11
Details	binding site for residue CO8 F 802

Chain	Residue
E	VAL596
E	ALA605
E	ASN606
E	TYR607
E	LYS636
F	PHE563
F	HIS566
F	PHE577
F	ARG613
F	PHE614
F	ILE615

site_id	AD3
Number of Residues	23
Details	binding site for residue NAP F 801

Chain	Residue
F	ARG20
F	ILE154
F	ASN155
F	ALA156
F	PHE157
F	ASN158
F	LYS181
F	ALA183
F	THR184
F	PHE230
F	THR231
F	GLY232
F	SER233
F	THR236
F	LEU240
F	GLU256
F	ALA257
F	ASP258
F	CYS295
F	GLU395
F	PHE397
F	LEU423
F	HIS472

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	666
Details	Domain: {"description":"MaoC-like"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	168
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	66
Details	Compositional bias: {"description":"Gly residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	12
Details	Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)