4IGN

2.32 Angstrom X-ray Crystal structure of R47A mutant of human ACMSD

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001760	molecular_function	aminocarboxymuconate-semialdehyde decarboxylase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006569	biological_process	L-tryptophan catabolic process
A	0008270	molecular_function	zinc ion binding
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	0046872	molecular_function	metal ion binding
A	1904985	biological_process	negative regulation of quinolinate biosynthetic process
A	1905004	biological_process	picolinic acid biosynthetic process
A	1905012	biological_process	regulation of 'de novo' NAD biosynthetic process from L-tryptophan
B	0001760	molecular_function	aminocarboxymuconate-semialdehyde decarboxylase activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006569	biological_process	L-tryptophan catabolic process
B	0008270	molecular_function	zinc ion binding
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	0046872	molecular_function	metal ion binding
B	1904985	biological_process	negative regulation of quinolinate biosynthetic process
B	1905004	biological_process	picolinic acid biosynthetic process
B	1905012	biological_process	regulation of 'de novo' NAD biosynthetic process from L-tryptophan
C	0001760	molecular_function	aminocarboxymuconate-semialdehyde decarboxylase activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006569	biological_process	L-tryptophan catabolic process
C	0008270	molecular_function	zinc ion binding
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	0046872	molecular_function	metal ion binding
C	1904985	biological_process	negative regulation of quinolinate biosynthetic process
C	1905004	biological_process	picolinic acid biosynthetic process
C	1905012	biological_process	regulation of 'de novo' NAD biosynthetic process from L-tryptophan
D	0001760	molecular_function	aminocarboxymuconate-semialdehyde decarboxylase activity
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006569	biological_process	L-tryptophan catabolic process
D	0008270	molecular_function	zinc ion binding
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	0046872	molecular_function	metal ion binding
D	1904985	biological_process	negative regulation of quinolinate biosynthetic process
D	1905004	biological_process	picolinic acid biosynthetic process
D	1905012	biological_process	regulation of 'de novo' NAD biosynthetic process from L-tryptophan
E	0001760	molecular_function	aminocarboxymuconate-semialdehyde decarboxylase activity
E	0005515	molecular_function	protein binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006569	biological_process	L-tryptophan catabolic process
E	0008270	molecular_function	zinc ion binding
E	0016787	molecular_function	hydrolase activity
E	0016829	molecular_function	lyase activity
E	0016831	molecular_function	carboxy-lyase activity
E	0019748	biological_process	secondary metabolic process
E	0046872	molecular_function	metal ion binding
E	1904985	biological_process	negative regulation of quinolinate biosynthetic process
E	1905004	biological_process	picolinic acid biosynthetic process
E	1905012	biological_process	regulation of 'de novo' NAD biosynthetic process from L-tryptophan
F	0001760	molecular_function	aminocarboxymuconate-semialdehyde decarboxylase activity
F	0005515	molecular_function	protein binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006569	biological_process	L-tryptophan catabolic process
F	0008270	molecular_function	zinc ion binding
F	0016787	molecular_function	hydrolase activity
F	0016829	molecular_function	lyase activity
F	0016831	molecular_function	carboxy-lyase activity
F	0019748	biological_process	secondary metabolic process
F	0046872	molecular_function	metal ion binding
F	1904985	biological_process	negative regulation of quinolinate biosynthetic process
F	1905004	biological_process	picolinic acid biosynthetic process
F	1905012	biological_process	regulation of 'de novo' NAD biosynthetic process from L-tryptophan

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 401

Chain	Residue
A	HIS6
A	HIS8
A	HIS174
A	ASP291
A	HOH638

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B 401

Chain	Residue
B	HOH666
B	HIS6
B	HIS8
B	HIS174
B	ASP291

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN C 401

Chain	Residue
C	HIS6
C	HIS8
C	HIS174
C	ASP291
C	HOH647

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN D 401

Chain	Residue
D	HIS6
D	HIS8
D	HIS174
D	ASP291
D	HOH644

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN E 401

Chain	Residue
E	HIS6
E	HIS8
E	HIS174
E	ASP291
E	HOH627

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN F 401

Chain	Residue
F	HIS6
F	HIS8
F	HIS174
F	ASP291
F	HOH582

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19843166","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19843166","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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