3KXP

Crystal Structure of E-2-(Acetamidomethylene)succinate Hydrolase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016787	molecular_function	hydrolase activity
A	0042803	molecular_function	protein homodimerization activity
A	0042820	biological_process	vitamin B6 catabolic process
A	0047411	molecular_function	2-(acetamidomethylene)succinate hydrolase activity
B	0016787	molecular_function	hydrolase activity
B	0042803	molecular_function	protein homodimerization activity
B	0042820	biological_process	vitamin B6 catabolic process
B	0047411	molecular_function	2-(acetamidomethylene)succinate hydrolase activity
C	0016787	molecular_function	hydrolase activity
C	0042803	molecular_function	protein homodimerization activity
C	0042820	biological_process	vitamin B6 catabolic process
C	0047411	molecular_function	2-(acetamidomethylene)succinate hydrolase activity
D	0016787	molecular_function	hydrolase activity
D	0042803	molecular_function	protein homodimerization activity
D	0042820	biological_process	vitamin B6 catabolic process
D	0047411	molecular_function	2-(acetamidomethylene)succinate hydrolase activity
E	0016787	molecular_function	hydrolase activity
E	0042803	molecular_function	protein homodimerization activity
E	0042820	biological_process	vitamin B6 catabolic process
E	0047411	molecular_function	2-(acetamidomethylene)succinate hydrolase activity
F	0016787	molecular_function	hydrolase activity
F	0042803	molecular_function	protein homodimerization activity
F	0042820	biological_process	vitamin B6 catabolic process
F	0047411	molecular_function	2-(acetamidomethylene)succinate hydrolase activity
G	0016787	molecular_function	hydrolase activity
G	0042803	molecular_function	protein homodimerization activity
G	0042820	biological_process	vitamin B6 catabolic process
G	0047411	molecular_function	2-(acetamidomethylene)succinate hydrolase activity
H	0016787	molecular_function	hydrolase activity
H	0042803	molecular_function	protein homodimerization activity
H	0042820	biological_process	vitamin B6 catabolic process
H	0047411	molecular_function	2-(acetamidomethylene)succinate hydrolase activity
I	0016787	molecular_function	hydrolase activity
I	0042803	molecular_function	protein homodimerization activity
I	0042820	biological_process	vitamin B6 catabolic process
I	0047411	molecular_function	2-(acetamidomethylene)succinate hydrolase activity
J	0016787	molecular_function	hydrolase activity
J	0042803	molecular_function	protein homodimerization activity
J	0042820	biological_process	vitamin B6 catabolic process
J	0047411	molecular_function	2-(acetamidomethylene)succinate hydrolase activity
K	0016787	molecular_function	hydrolase activity
K	0042803	molecular_function	protein homodimerization activity
K	0042820	biological_process	vitamin B6 catabolic process
K	0047411	molecular_function	2-(acetamidomethylene)succinate hydrolase activity
L	0016787	molecular_function	hydrolase activity
L	0042803	molecular_function	protein homodimerization activity
L	0042820	biological_process	vitamin B6 catabolic process
L	0047411	molecular_function	2-(acetamidomethylene)succinate hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 279

Chain	Residue
A	ILE41
A	SER106
A	LEU107
A	HOH630

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL B 279

Chain	Residue
B	ILE41
B	SER106
B	LEU107
B	HOH455

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL C 279

Chain	Residue
C	SER106
C	LEU107
C	HOH737
C	ILE41

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL D 279

Chain	Residue
D	ILE41
D	SER106
D	LEU107
D	HOH339

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL E 279

Chain	Residue
E	ILE41
E	SER106
E	LEU107
E	HOH794

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL F 279

Chain	Residue
F	ILE41
F	SER106
F	LEU107
F	LEU207
F	HOH432

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL G 279

Chain	Residue
G	ILE41
G	SER106
G	LEU107
G	HOH375

---

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL H 279

Chain	Residue
H	ILE41
H	SER106
H	LEU107

---

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL I 279

Chain	Residue
I	ILE41
I	SER106
I	LEU107

---

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL J 279

Chain	Residue
J	ILE41
J	SER106
J	LEU107

---

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL K 279

Chain	Residue
K	ILE41
K	SER106
K	LEU107
K	HOH1381

---

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL L 279

Chain	Residue
L	ILE41
L	SER106
L	LEU107
L	HOH308

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"20099871","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	Active site: {"evidences":[{"source":"PubMed","id":"20099871","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20099871","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {}

Chain

Residue

Details

---