6DXS

Crystal structure of the LigJ hydratase E284Q mutant substrate complex with (3Z)-2-keto-4-carboxy-3-hexenedioate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0016787	molecular_function	hydrolase activity
A	0016829	molecular_function	lyase activity
A	0016831	molecular_function	carboxy-lyase activity
A	0019748	biological_process	secondary metabolic process
A	0046274	biological_process	lignin catabolic process
A	0046872	molecular_function	metal ion binding
B	0005737	cellular_component	cytoplasm
B	0016787	molecular_function	hydrolase activity
B	0016829	molecular_function	lyase activity
B	0016831	molecular_function	carboxy-lyase activity
B	0019748	biological_process	secondary metabolic process
B	0046274	biological_process	lignin catabolic process
B	0046872	molecular_function	metal ion binding
C	0005737	cellular_component	cytoplasm
C	0016787	molecular_function	hydrolase activity
C	0016829	molecular_function	lyase activity
C	0016831	molecular_function	carboxy-lyase activity
C	0019748	biological_process	secondary metabolic process
C	0046274	biological_process	lignin catabolic process
C	0046872	molecular_function	metal ion binding
D	0005737	cellular_component	cytoplasm
D	0016787	molecular_function	hydrolase activity
D	0016829	molecular_function	lyase activity
D	0016831	molecular_function	carboxy-lyase activity
D	0019748	biological_process	secondary metabolic process
D	0046274	biological_process	lignin catabolic process
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue ZN A 401

Chain	Residue
A	HIS8
A	HIS10
A	HIS178
A	GLN284
A	HJ7402

---

site_id	AC2
Number of Residues	15
Details	binding site for residue HJ7 A 402

Chain	Residue
A	ALA72
A	SER73
A	THR190
A	TYR194
A	HIS223
A	GLN284
A	ALA288
A	ARG290
A	ZN401
A	HOH556
D	ARG234
A	HIS8
A	HIS10
A	THR12
A	ARG71

---

site_id	AC3
Number of Residues	4
Details	binding site for residue ZN B 401

Chain	Residue
B	HIS8
B	HIS10
B	HIS178
B	HJ7402

---

site_id	AC4
Number of Residues	17
Details	binding site for residue HJ7 B 402

Chain	Residue
B	HIS8
B	HIS10
B	THR12
B	ARG71
B	ALA72
B	SER73
B	HIS178
B	TYR194
B	HIS223
B	GLN284
B	GLY287
B	ALA288
B	ARG290
B	ZN401
B	HOH538
B	HOH553
C	ARG234

---

site_id	AC5
Number of Residues	4
Details	binding site for residue ZN C 401

Chain	Residue
C	HIS8
C	HIS10
C	HIS178
C	HJ7402

---

site_id	AC6
Number of Residues	17
Details	binding site for residue HJ7 C 402

Chain	Residue
B	ARG234
C	HIS8
C	HIS10
C	THR12
C	ARG71
C	ALA72
C	SER73
C	HIS178
C	TYR194
C	HIS223
C	GLN284
C	GLY287
C	ALA288
C	ARG290
C	ZN401
C	HOH531
C	HOH564

---

site_id	AC7
Number of Residues	4
Details	binding site for residue ZN D 401

Chain	Residue
D	HIS8
D	HIS10
D	HIS178
D	HJ7402

---

site_id	AC8
Number of Residues	15
Details	binding site for residue HJ7 D 402

Chain	Residue
A	ARG234
D	HIS8
D	HIS10
D	THR12
D	ARG71
D	ALA72
D	SER73
D	HIS178
D	TYR194
D	HIS223
D	GLN284
D	ARG290
D	ZN401
D	HOH548
D	HOH573

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"30207699","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"30207699","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6DWV","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"30207699","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6DXS","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

---