Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3M83

Crystal structure of Acetyl xylan esterase (TM0077) from THERMOTOGA MARITIMA at 2.12 A resolution (paraoxon inhibitor complex structure)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005509	molecular_function	calcium ion binding
A	0005737	cellular_component	cytoplasm
A	0005976	biological_process	polysaccharide metabolic process
A	0016788	molecular_function	hydrolase activity, acting on ester bonds
A	0030245	biological_process	cellulose catabolic process
A	0045491	biological_process	xylan metabolic process
A	0046555	molecular_function	acetylxylan esterase activity
A	0046872	molecular_function	metal ion binding
A	0047739	molecular_function	cephalosporin-C deacetylase activity
A	0052689	molecular_function	carboxylic ester hydrolase activity
A	1901266	biological_process	cephalosporin C metabolic process
B	0005509	molecular_function	calcium ion binding
B	0005737	cellular_component	cytoplasm
B	0005976	biological_process	polysaccharide metabolic process
B	0016788	molecular_function	hydrolase activity, acting on ester bonds
B	0030245	biological_process	cellulose catabolic process
B	0045491	biological_process	xylan metabolic process
B	0046555	molecular_function	acetylxylan esterase activity
B	0046872	molecular_function	metal ion binding
B	0047739	molecular_function	cephalosporin-C deacetylase activity
B	0052689	molecular_function	carboxylic ester hydrolase activity
B	1901266	biological_process	cephalosporin C metabolic process
C	0005509	molecular_function	calcium ion binding
C	0005737	cellular_component	cytoplasm
C	0005976	biological_process	polysaccharide metabolic process
C	0016788	molecular_function	hydrolase activity, acting on ester bonds
C	0030245	biological_process	cellulose catabolic process
C	0045491	biological_process	xylan metabolic process
C	0046555	molecular_function	acetylxylan esterase activity
C	0046872	molecular_function	metal ion binding
C	0047739	molecular_function	cephalosporin-C deacetylase activity
C	0052689	molecular_function	carboxylic ester hydrolase activity
C	1901266	biological_process	cephalosporin C metabolic process
D	0005509	molecular_function	calcium ion binding
D	0005737	cellular_component	cytoplasm
D	0005976	biological_process	polysaccharide metabolic process
D	0016788	molecular_function	hydrolase activity, acting on ester bonds
D	0030245	biological_process	cellulose catabolic process
D	0045491	biological_process	xylan metabolic process
D	0046555	molecular_function	acetylxylan esterase activity
D	0046872	molecular_function	metal ion binding
D	0047739	molecular_function	cephalosporin-C deacetylase activity
D	0052689	molecular_function	carboxylic ester hydrolase activity
D	1901266	biological_process	cephalosporin C metabolic process
E	0005509	molecular_function	calcium ion binding
E	0005737	cellular_component	cytoplasm
E	0005976	biological_process	polysaccharide metabolic process
E	0016788	molecular_function	hydrolase activity, acting on ester bonds
E	0030245	biological_process	cellulose catabolic process
E	0045491	biological_process	xylan metabolic process
E	0046555	molecular_function	acetylxylan esterase activity
E	0046872	molecular_function	metal ion binding
E	0047739	molecular_function	cephalosporin-C deacetylase activity
E	0052689	molecular_function	carboxylic ester hydrolase activity
E	1901266	biological_process	cephalosporin C metabolic process
F	0005509	molecular_function	calcium ion binding
F	0005737	cellular_component	cytoplasm
F	0005976	biological_process	polysaccharide metabolic process
F	0016788	molecular_function	hydrolase activity, acting on ester bonds
F	0030245	biological_process	cellulose catabolic process
F	0045491	biological_process	xylan metabolic process
F	0046555	molecular_function	acetylxylan esterase activity
F	0046872	molecular_function	metal ion binding
F	0047739	molecular_function	cephalosporin-C deacetylase activity
F	0052689	molecular_function	carboxylic ester hydrolase activity
F	1901266	biological_process	cephalosporin C metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 401

Chain	Residue
A	GLU45
A	ASP58
A	HOH448
A	HOH477
A	HOH695
C	GLU45

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 404

Chain	Residue
A	HOH989
A	HOH1292
A	HOH1400
A	LYS22
A	GLU26
A	HOH576

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 417

Chain	Residue
A	GLN88
A	TRP105
A	GLY186
A	GLY187
A	ASP210
A	GLN314
A	HOH726

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 418

Chain	Residue
A	GLY123
A	TRP124
A	HOH1049
C	LYS237
C	THR238

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 422

Chain	Residue
A	TYR110
A	ARG181
A	HOH633

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA B 408

Chain	Residue
B	LYS22
B	GLU26
B	HOH586
B	HOH706

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO B 413

Chain	Residue
B	GLN88
B	TRP105
B	ALA185
B	GLY186
B	GLY187
B	ASP210
B	GLN314

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 403

Chain	Residue
C	LYS22
C	GLU26
C	HOH499
C	HOH885
C	HOH1195
C	HOH1248

site_id	AC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ACT C 409

Chain	Residue
A	GLN140
A	PRO142
A	GLY143
A	ARG147
C	GLN140
C	PRO142
C	GLY143
C	PHE144
C	ARG147
C	HOH1300

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO C 412

Chain	Residue
C	GLN88
C	TRP105
C	GLY186
C	GLY187
C	ASP210
C	GLN314
C	HOH1143

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO C 421

Chain	Residue
C	TYR110
C	ARG181
C	HOH715
C	HOH1023

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO C 423

Chain	Residue
C	LYS316
C	LYS319
E	HIS50

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 402

Chain	Residue
B	GLU45
D	GLU45
D	ASP58
D	HOH520
D	HOH673
D	HOH712

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA D 405

Chain	Residue
D	LYS22
D	GLU26
D	HOH582
D	HOH1330

site_id	BC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ACT D 410

Chain	Residue
B	GLN140
B	PRO142
B	GLY143
B	ARG147
D	GLN140
D	PRO142
D	GLY143
D	PHE144
D	ARG147
D	HOH1243

site_id	BC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO D 414

Chain	Residue
D	GLN88
D	TRP105
D	ALA185
D	GLY186
D	GLY187
D	ASP210
D	GLN314
D	HOH1000

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO D 420

Chain	Residue
D	HOH900
D	HOH1009
D	TYR110
D	ARG181
D	PHE322

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA E 407

Chain	Residue
E	LYS22
E	GLU26
E	HOH711
E	HOH1302

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO E 415

Chain	Residue
E	GLN88
E	TRP105
E	ALA185
E	GLY186
E	GLY187
E	ASP210

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA F 406

Chain	Residue
F	LYS22
F	GLU26
F	HOH741
F	HOH1405

site_id	CC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ACT F 411

Chain	Residue
E	GLN140
E	PRO142
E	GLY143
E	ARG147
F	GLN140
F	PRO142
F	GLY143
F	PHE144
F	ARG147
F	HOH1142

site_id	CC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO F 416

Chain	Residue
F	GLN88
F	TRP105
F	ALA185
F	GLY186
F	GLY187
F	ASP210
F	GLN314

site_id	CC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO F 419

Chain	Residue
F	TYR110
F	ARG181
F	PHE322
F	HOH721
F	HOH901

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: Nucleophile => ECO:0000269\|PubMed:22411095

Chain	Residue	Details
A	SDP188
B	SDP188
C	SDP188
D	SDP188
E	SDP188
F	SDP188

site_id	SWS_FT_FI2
Number of Residues	12
Details	ACT_SITE: Charge relay system => ECO:0000250\|UniProtKB:P94388

Chain	Residue	Details
A	ASP274
E	HIS303
F	ASP274
F	HIS303
A	HIS303
B	ASP274
B	HIS303
C	ASP274
C	HIS303
D	ASP274
D	HIS303
E	ASP274

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P94388

Chain	Residue	Details
A	TYR92
B	TYR92
C	TYR92
D	TYR92
E	TYR92
F	TYR92

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: covalent => ECO:0000269\|PubMed:22411095

Chain	Residue	Details
A	SDP188
B	SDP188
C	SDP188
D	SDP188
E	SDP188
F	SDP188

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