6GBJ

Repertoires of functionally diverse enzymes through computational design at epistatic active-site positions

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004063	molecular_function	aryldialkylphosphatase activity
A	0005886	cellular_component	plasma membrane
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue FMT A 401

Chain	Residue
A	HIS55
A	HOH530
A	HIS57
A	TRP131
A	LYS169
A	HIS201
A	HIS230
A	ZN402
A	ZN403
A	EDO405

---

site_id	AC2
Number of Residues	7
Details	binding site for residue ZN A 402

Chain	Residue
A	HIS55
A	HIS57
A	ASP301
A	FMT401
A	ZN403
A	EDO405
A	HOH530

---

site_id	AC3
Number of Residues	8
Details	binding site for residue ZN A 403

Chain	Residue
A	HIS201
A	HIS230
A	ARG254
A	FMT401
A	ZN402
A	EDO405
A	HOH502
A	HOH530

---

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

Chain	Residue
A	HIS57
A	GLY60
A	TRP257
A	ASP301
A	THR303
A	PHE306
A	EDO405
A	HOH526

---

site_id	AC5
Number of Residues	10
Details	binding site for residue EDO A 405

Chain	Residue
A	HIS57
A	TRP131
A	FMT401
A	ZN402
A	ZN403
A	EDO404
A	EDO407
A	HOH502
A	HOH526
A	HOH530

---

site_id	AC6
Number of Residues	7
Details	binding site for residue EDO A 406

Chain	Residue
A	TYR156
A	GLY157
A	ILE158
A	GLU159
A	ASP160
A	THR161
A	GLY162

---

site_id	AC7
Number of Residues	7
Details	binding site for residue EDO A 407

Chain	Residue
A	TRP131
A	HIS201
A	ARG254
A	EDO405
A	HOH502
A	HOH503
A	HOH529

---

site_id	AC8
Number of Residues	8
Details	binding site for residue EDO A 408

Chain	Residue
A	PRO70
A	SER75
A	ARG76
A	ASP77
A	ARG363
A	HOH506
A	HOH680
A	HOH701

---

site_id	AC9
Number of Residues	7
Details	binding site for residue EDO A 409

Chain	Residue
A	ASP233
A	ARG254
A	LEU271
A	LEU272
A	ARG280
A	HOH598
A	HOH608

---

site_id	AD1
Number of Residues	4
Details	binding site for residue EDO A 410

Chain	Residue
A	LYS175
A	ALA176
A	GLU181
A	GLN211

---

site_id	AD2
Number of Residues	7
Details	binding site for residue EDO A 411

Chain	Residue
A	PRO256
A	TRP277
A	VAL320
A	ASN321
A	PHE327
A	HOH578
A	HOH584

---

site_id	AD3
Number of Residues	4
Details	binding site for residue SO4 A 412

Chain	Residue
A	LYS82
A	ARG85
A	ARG89
A	HOH537

---

site_id	AD4
Number of Residues	2
Details	binding site for residue SO4 A 413

Chain	Residue
A	TRP277
A	GLN278

---

site_id	AD5
Number of Residues	3
Details	binding site for residue SO4 A 414

Chain	Residue
A	ARG139
A	HOH549
A	HOH582

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY50-ILE58

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7794910","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DPM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EYW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EZ2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1HZY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O4M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O4Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OB3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OQL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Binding site: {"description":"via carbamate group","evidences":[{"source":"PubMed","id":"7794910","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DPM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EYW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EZ2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1HZY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O4M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O4Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OB3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OQL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00679","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7794910","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DPM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EYW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EZ2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1HZY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O4M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O4Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OB3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OQL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	8
Details	M-CSA 159

Chain	Residue	Details
A	HIS55	metal ligand
A	HIS57	metal ligand
A	LYS169	metal ligand
A	HIS201	metal ligand
A	HIS230	metal ligand
A	ASP233	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ARG254	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	ASP301	hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor

---