Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2O4M

Structure of Phosphotriesterase mutant I106G/F132G/H257Y

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
B	0004063	molecular_function	aryldialkylphosphatase activity
B	0005886	cellular_component	plasma membrane
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	0005886	cellular_component	plasma membrane
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
P	0004063	molecular_function	aryldialkylphosphatase activity
P	0005886	cellular_component	plasma membrane
P	0008270	molecular_function	zinc ion binding
P	0009056	biological_process	catabolic process
P	0016787	molecular_function	hydrolase activity
P	0016788	molecular_function	hydrolase activity, acting on ester bonds
P	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 3001

Chain	Residue
A	HIS55
A	HIS57
A	KCX169
A	ASP301
A	CAC4001

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN P 3002

Chain	Residue
P	CAC4004
P	HIS55
P	HIS57
P	KCX169
P	ASP301

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 3003

Chain	Residue
A	KCX169
A	HIS201
A	HIS230
A	CAC4001

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN P 3004

Chain	Residue
P	KCX169
P	HIS201
P	HIS230
P	CAC4004

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B 3005

Chain	Residue
B	HIS55
B	HIS57
B	KCX169
B	ASP301
B	CAC4002

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 3006

Chain	Residue
B	KCX169
B	HIS201
B	HIS230
B	CAC4002

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN C 3007

Chain	Residue
C	HIS55
C	HIS57
C	KCX169
C	ASP301
C	CAC4003

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 3008

Chain	Residue
C	KCX169
C	HIS201
C	HIS230
C	CAC4003

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 3009

Chain	Residue
A	ASP233
A	HIS254
A	ACY6003
A	HOH6210
A	HOH6223

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 3010

Chain	Residue
B	ASP233
B	HIS254
B	ACY6002
B	HOH6139

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN P 3011

Chain	Residue
P	ASP233
P	HIS254
P	GOL5003
P	HOH5139
P	HOH5143

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN P 3012

Chain	Residue
P	GLU48
P	HIS123
P	HOH5097
P	HOH5192

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ZN A 3013

Chain	Residue
A	GLU48
A	HIS123

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 3014

Chain	Residue
B	GLU48
B	HIS123
B	GOL5002
B	HOH6265

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 3015

Chain	Residue
C	GLU48
C	HIS123
C	GOL5004
C	HOH6279

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN C 3016

Chain	Residue
C	ASP233
C	HIS254
C	ACY6001
C	HOH6132
C	HOH6201

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 3017

Chain	Residue
B	ASP160
C	GLU344
C	GOL5005
C	HOH6133

site_id	BC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ZN A 3018

Chain	Residue
A	GLU344
P	ASP160

site_id	CC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN B 3019

Chain	Residue
B	GLU344
B	HOH6338
C	ASP160

site_id	CC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN C 3020

Chain	Residue
C	ASP236
C	SER238
C	HOH6149

site_id	CC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ZN P 3021

Chain	Residue
P	GLN343
P	GLU344

site_id	CC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ZN P 3022

Chain	Residue
P	ASP121
P	HOH5307

site_id	CC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 3024

Chain	Residue
A	ARG207
A	ASP236
A	SER238
A	HOH6305

site_id	CC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CAC A 4001

Chain	Residue
A	HIS55
A	HIS57
A	TRP131
A	KCX169
A	HIS201
A	HIS230
A	ASP301
A	ZN3001
A	ZN3003

site_id	CC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CAC B 4002

Chain	Residue
B	HIS57
B	TRP131
B	KCX169
B	HIS201
B	HIS230
B	ASP301
B	ZN3005
B	ZN3006
B	ACY6002
B	HIS55

site_id	CC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CAC C 4003

Chain	Residue
C	HIS55
C	HIS57
C	TRP131
C	KCX169
C	HIS201
C	HIS230
C	ASP301
C	ZN3007
C	ZN3008

site_id	CC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CAC P 4004

Chain	Residue
P	HIS55
P	HIS57
P	TRP131
P	KCX169
P	HIS201
P	HIS230
P	ASP301
P	ZN3002
P	ZN3004

site_id	DC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL P 5001

Chain	Residue
A	GLY94
A	ARG96
A	HOH6111
P	GLN155
P	TYR156
P	HOH5217

site_id	DC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 5002

Chain	Residue
B	GLU48
B	ASP121
B	HIS123
B	ZN3014
B	HOH6138

site_id	DC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL P 5003

Chain	Residue
P	HIS201
P	HIS230
P	ASP233
P	HIS254
P	TYR257
P	LEU271
P	ZN3011
P	HOH5139
P	HOH5186

site_id	DC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 5004

Chain	Residue
C	GLU48
C	ARG96
C	ASP121
C	HIS123
C	ZN3015
C	HOH6210

site_id	DC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 5005

Chain	Residue
B	ASP160
B	THR161
C	PRO342
C	GLN343
C	GLU344
C	ZN3017
C	HOH6133

site_id	DC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACY C 6001

Chain	Residue
C	HIS230
C	ASP233
C	HIS254
C	LEU271
C	ZN3016
C	HOH6132
C	HOH6223

site_id	DC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ACY B 6002

Chain	Residue
B	HIS230
B	ASP233
B	HIS254
B	LEU271
B	ZN3010
B	CAC4002
B	HOH6139
B	HOH6220

site_id	DC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACY A 6003

Chain	Residue
A	HIS230
A	ASP233
A	HIS254
A	LEU271
A	ZN3009
A	HOH6129

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY50-ILE58

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
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	4
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	4
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	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1ez2

Chain	Residue	Details
A	HIS254
A	ASP233
A	ASP301

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1ez2

Chain	Residue	Details
B	HIS254
B	ASP233
B	ASP301

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ez2

Chain	Residue	Details
C	HIS254
C	ASP233
C	ASP301

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1ez2

Chain	Residue	Details
P	HIS254
P	ASP233
P	ASP301

site_id	MCSA1
Number of Residues	8
Details	M-CSA 159

Chain	Residue	Details
A	HIS55	metal ligand
A	HIS57	metal ligand
A	KCX169	metal ligand
A	SER205	metal ligand
A	THR234	metal ligand
A	LEU237	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	SER258	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	GLY305	hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor

site_id	MCSA2
Number of Residues	8
Details	M-CSA 159

Chain	Residue	Details
B	HIS55	metal ligand
B	HIS57	metal ligand
B	KCX169	metal ligand
B	SER205	metal ligand
B	THR234	metal ligand
B	LEU237	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	SER258	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	GLY305	hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor

site_id	MCSA3
Number of Residues	8
Details	M-CSA 159

Chain	Residue	Details
C	HIS55	metal ligand
C	HIS57	metal ligand
C	KCX169	metal ligand
C	SER205	metal ligand
C	THR234	metal ligand
C	LEU237	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	SER258	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
C	GLY305	hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor

site_id	MCSA4
Number of Residues	8
Details	M-CSA 159

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)