5VSA

Crystal structure of SsoPox AsA1 mutant (C258L-I261F-W263A)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004063	molecular_function	aryldialkylphosphatase activity
A	0008270	molecular_function	zinc ion binding
A	0009056	biological_process	catabolic process
A	0016787	molecular_function	hydrolase activity
A	0016788	molecular_function	hydrolase activity, acting on ester bonds
A	0046872	molecular_function	metal ion binding
B	0004063	molecular_function	aryldialkylphosphatase activity
B	0008270	molecular_function	zinc ion binding
B	0009056	biological_process	catabolic process
B	0016787	molecular_function	hydrolase activity
B	0016788	molecular_function	hydrolase activity, acting on ester bonds
B	0046872	molecular_function	metal ion binding
C	0004063	molecular_function	aryldialkylphosphatase activity
C	0008270	molecular_function	zinc ion binding
C	0009056	biological_process	catabolic process
C	0016787	molecular_function	hydrolase activity
C	0016788	molecular_function	hydrolase activity, acting on ester bonds
C	0046872	molecular_function	metal ion binding
D	0004063	molecular_function	aryldialkylphosphatase activity
D	0008270	molecular_function	zinc ion binding
D	0009056	biological_process	catabolic process
D	0016787	molecular_function	hydrolase activity
D	0016788	molecular_function	hydrolase activity, acting on ester bonds
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue FE2 A 401

Chain	Residue
A	HIS22
A	HIS24
A	KCX137
A	ASP256
A	CO402
A	GOL405
A	HOH506

---

site_id	AC2
Number of Residues	6
Details	binding site for residue CO A 402

Chain	Residue
A	HIS199
A	FE2401
A	GOL405
A	HOH506
A	KCX137
A	HIS170

---

site_id	AC3
Number of Residues	7
Details	binding site for residue GOL A 403

Chain	Residue
A	ASN160
A	LYS164
A	VAL190
A	ASP191
A	LYS194
A	HOH544
A	HOH585

---

site_id	AC4
Number of Residues	8
Details	binding site for residue GOL A 404

Chain	Residue
A	PRO4
A	LEU5
A	LYS8
A	ASP9
A	SER10
A	LEU130
A	ASN131
A	LYS132

---

site_id	AC5
Number of Residues	7
Details	binding site for residue GOL A 405

Chain	Residue
A	HIS24
A	TYR97
A	KCX137
A	ASP256
A	FE2401
A	CO402
A	HOH506

---

site_id	AC6
Number of Residues	7
Details	binding site for residue FE2 B 401

Chain	Residue
B	HIS22
B	HIS24
B	KCX137
B	ASP256
B	CO402
B	HOH506
B	HOH660

---

site_id	AC7
Number of Residues	6
Details	binding site for residue CO B 402

Chain	Residue
B	KCX137
B	HIS170
B	HIS199
B	FE2401
B	HOH506
B	HOH625

---

site_id	AC8
Number of Residues	10
Details	binding site for residue GOL B 403

Chain	Residue
B	PRO4
B	LEU5
B	LYS8
B	ASP9
B	SER10
B	LEU130
B	ASN131
B	LYS132
B	HOH596
B	HOH609

---

site_id	AC9
Number of Residues	6
Details	binding site for residue GOL B 404

Chain	Residue
B	ASN160
B	LYS164
B	GLY189
B	VAL190
B	ASP191
B	HOH543

---

site_id	AD1
Number of Residues	7
Details	binding site for residue FE2 C 401

Chain	Residue
C	HIS22
C	HIS24
C	KCX137
C	ASP256
C	CO402
C	GOL404
C	HOH518

---

site_id	AD2
Number of Residues	6
Details	binding site for residue CO C 402

Chain	Residue
C	KCX137
C	HIS170
C	HIS199
C	FE2401
C	GOL404
C	HOH518

---

site_id	AD3
Number of Residues	6
Details	binding site for residue GOL C 403

Chain	Residue
C	ASN160
C	LYS164
C	GLY189
C	VAL190
C	ASP191
C	HOH517

---

site_id	AD4
Number of Residues	11
Details	binding site for residue GOL C 404

Chain	Residue
C	HIS24
C	TYR97
C	TYR99
C	KCX137
C	HIS170
C	ARG223
C	ASP256
C	FE2401
C	CO402
C	HOH518
C	HOH613

---

site_id	AD5
Number of Residues	6
Details	binding site for residue FE2 D 401

Chain	Residue
D	HOH510
D	HIS22
D	HIS24
D	KCX137
D	ASP256
D	CO402

---

site_id	AD6
Number of Residues	6
Details	binding site for residue CO D 402

Chain	Residue
D	KCX137
D	HIS170
D	HIS199
D	FE2401
D	HOH510
D	HOH579

---

site_id	AD7
Number of Residues	5
Details	binding site for residue GOL D 403

Chain	Residue
D	ASN160
D	LYS164
D	GLY189
D	ASP191
D	LYS194

---

Functional Information from PROSITE/UniProt

site_id	PS01322
Number of Residues	9
Details	PHOSPHOTRIESTERASE_1 Phosphotriesterase family signature 1. GfTLiHEHL

Chain	Residue	Details
A	GLY17-LEU25

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269|PubMed:18486146, ECO:0007744|PDB:2VC5, ECO:0007744|PDB:2VC7, ECO:0007744|PDB:3UF9, ECO:0007744|PDB:4KER, ECO:0007744|PDB:4KES, ECO:0007744|PDB:4KET, ECO:0007744|PDB:4KEU, ECO:0007744|PDB:4KEV, ECO:0007744|PDB:4KEZ, ECO:0007744|PDB:4KF1

Chain	Residue	Details
B	HIS199
B	ASP256
C	HIS22
C	HIS24
C	HIS170
C	HIS199
C	ASP256
D	HIS22
D	HIS24
D	HIS170
D	HIS199
D	ASP256
A	HIS170
A	HIS199
A	ASP256
B	HIS22
B	HIS24
B	HIS170
A	HIS22
A	HIS24

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: via carbamate group => ECO:0000269|PubMed:18486146, ECO:0007744|PDB:2VC5, ECO:0007744|PDB:2VC7, ECO:0007744|PDB:3UF9, ECO:0007744|PDB:4KER, ECO:0007744|PDB:4KES, ECO:0007744|PDB:4KET, ECO:0007744|PDB:4KEU, ECO:0007744|PDB:4KEV, ECO:0007744|PDB:4KEZ, ECO:0007744|PDB:4KF1

Chain	Residue	Details
A	KCX137
B	KCX137
C	KCX137
D	KCX137

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: N6-carboxylysine => ECO:0000255|PROSITE-ProRule:PRU00679, ECO:0000269|PubMed:18486146, ECO:0007744|PDB:2VC5, ECO:0007744|PDB:2VC7, ECO:0007744|PDB:3UF9, ECO:0007744|PDB:4KER, ECO:0007744|PDB:4KES, ECO:0007744|PDB:4KET, ECO:0007744|PDB:4KEU, ECO:0007744|PDB:4KEV, ECO:0007744|PDB:4KEZ, ECO:0007744|PDB:4KF1

Chain	Residue	Details
A	KCX137
B	KCX137
C	KCX137
D	KCX137

---