Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3DD5

Glomerella cingulata E600-cutinase complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0016787	molecular_function	hydrolase activity
A	0050525	molecular_function	cutinase activity
A	0052689	molecular_function	carboxylic ester hydrolase activity
B	0005576	cellular_component	extracellular region
B	0016787	molecular_function	hydrolase activity
B	0050525	molecular_function	cutinase activity
B	0052689	molecular_function	carboxylic ester hydrolase activity
C	0005576	cellular_component	extracellular region
C	0016787	molecular_function	hydrolase activity
C	0050525	molecular_function	cutinase activity
C	0052689	molecular_function	carboxylic ester hydrolase activity
D	0005576	cellular_component	extracellular region
D	0016787	molecular_function	hydrolase activity
D	0050525	molecular_function	cutinase activity
D	0052689	molecular_function	carboxylic ester hydrolase activity
E	0005576	cellular_component	extracellular region
E	0016787	molecular_function	hydrolase activity
E	0050525	molecular_function	cutinase activity
E	0052689	molecular_function	carboxylic ester hydrolase activity
F	0005576	cellular_component	extracellular region
F	0016787	molecular_function	hydrolase activity
F	0050525	molecular_function	cutinase activity
F	0052689	molecular_function	carboxylic ester hydrolase activity
G	0005576	cellular_component	extracellular region
G	0016787	molecular_function	hydrolase activity
G	0050525	molecular_function	cutinase activity
G	0052689	molecular_function	carboxylic ester hydrolase activity
H	0005576	cellular_component	extracellular region
H	0016787	molecular_function	hydrolase activity
H	0050525	molecular_function	cutinase activity
H	0052689	molecular_function	carboxylic ester hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DEP A 401

Chain	Residue
A	ALA56
A	SER57
A	ASN100
A	SER136
A	GLN137

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE DEP B 402

Chain	Residue
B	SER57
B	ASN100
B	SER136
B	GLN137

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DEP C 403

Chain	Residue
C	ALA56
C	SER57
C	SER136
C	GLN137
C	PHE199

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE DEP D 404

Chain	Residue
D	ALA56
D	SER57
D	ASN100
D	TYR135
D	SER136
D	GLN137
D	VAL193
D	PHE199

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE DEP E 405

Chain	Residue
E	ALA56
E	SER57
E	ASN100
E	TYR135
E	SER136
E	GLN137
E	VAL193

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE DEP F 406

Chain	Residue
F	ALA56
F	SER57
F	ASN100
F	TYR135
F	SER136
F	GLN137
F	VAL193
F	LEU198

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE DEP G 407

Chain	Residue
G	ALA56
G	SER57
G	ASN100
G	TYR135
G	SER136
G	GLN137
G	LEU201

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE DEP H 408

Chain	Residue
H	ALA56
H	SER57
H	TYR135
H	SER136
H	GLN137
H	VAL193
H	PHE199

Functional Information from PROSITE/UniProt

site_id	PS00155
Number of Residues	13
Details	CUTINASE_1 Cutinase, serine active site. PnAaIVsGGYSQG

Chain	Residue	Details
A	PRO126-GLY138

site_id	PS00931
Number of Residues	18
Details	CUTINASE_2 Cutinase, aspartate and histidine active sites. CdiaDaVCyGTlfIlpaH

Chain	Residue	Details
A	CYS187-HIS204

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Nucleophile => ECO:0000305\|PubMed:18983850

Chain	Residue	Details
A	SER136
B	SER136
C	SER136
D	SER136
E	SER136
F	SER136
G	SER136
H	SER136

site_id	SWS_FT_FI2
Number of Residues	8
Details	ACT_SITE: ACT_SITE => ECO:0000305\|PubMed:18983850

Chain	Residue	Details
A	ASP191
B	ASP191
C	ASP191
D	ASP191
E	ASP191
F	ASP191
G	ASP191
H	ASP191

site_id	SWS_FT_FI3
Number of Residues	8
Details	ACT_SITE: Proton donor/acceptor => ECO:0000305\|PubMed:18983850

Chain	Residue	Details
A	HIS204
B	HIS204
C	HIS204
D	HIS204
E	HIS204
F	HIS204
G	HIS204
H	HIS204

site_id	SWS_FT_FI4
Number of Residues	16
Details	SITE: Transition state stabilizer => ECO:0000250\|UniProtKB:P00590

Chain	Residue	Details
A	SER57
E	GLN137
F	SER57
F	GLN137
G	SER57
G	GLN137
H	SER57
H	GLN137
A	GLN137
B	SER57
B	GLN137
C	SER57
C	GLN137
D	SER57
D	GLN137
E	SER57

Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1agy

Chain	Residue	Details
A	SER136
A	HIS204
A	GLN137
A	SER57
A	ASP191

site_id	CSA2
Number of Residues	5
Details	Annotated By Reference To The Literature 1agy

Chain	Residue	Details
B	SER136
B	HIS204
B	GLN137
B	SER57
B	ASP191

site_id	CSA3
Number of Residues	5
Details	Annotated By Reference To The Literature 1agy

Chain	Residue	Details
C	SER136
C	HIS204
C	GLN137
C	SER57
C	ASP191

site_id	CSA4
Number of Residues	5
Details	Annotated By Reference To The Literature 1agy

Chain	Residue	Details
D	SER136
D	HIS204
D	GLN137
D	SER57
D	ASP191

site_id	CSA5
Number of Residues	5
Details	Annotated By Reference To The Literature 1agy

Chain	Residue	Details
E	SER136
E	HIS204
E	GLN137
E	SER57
E	ASP191

site_id	CSA6
Number of Residues	5
Details	Annotated By Reference To The Literature 1agy

Chain	Residue	Details
F	SER136
F	HIS204
F	GLN137
F	SER57
F	ASP191

site_id	CSA7
Number of Residues	5
Details	Annotated By Reference To The Literature 1agy

Chain	Residue	Details
G	SER136
G	HIS204
G	GLN137
G	SER57
G	ASP191

site_id	CSA8
Number of Residues	5
Details	Annotated By Reference To The Literature 1agy

Chain	Residue	Details
H	SER136
H	HIS204
H	GLN137
H	SER57
H	ASP191

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