1XZC

FUSARIUM SOLANI CUTINASE MUTANT WITH SER 129 REPLACED BY CYS COMPLEX WITH PARA-SULFUROUSPHENYL MERCURY

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0016052	biological_process	carbohydrate catabolic process
A	0016787	molecular_function	hydrolase activity
A	0050525	molecular_function	cutinase activity
A	0052689	molecular_function	carboxylic ester hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PMB A 801

Chain	Residue
A	HOH645
A	ILE95
A	LEU99
A	CYS129
A	ASP132
A	LEU133
A	HOH554

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site_id	CAT
Number of Residues	3
Details	CATALYTIC TRIAD.

Chain	Residue
A	SER120
A	HIS188
A	ASP175

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PRO110-GLY122

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

Chain	Residue	Details
A	CYS171-HIS188

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:1560844, ECO:0007744|PDB:1AGY

Chain	Residue	Details
A	SER120

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: ACT_SITE => ECO:0000269|PubMed:1560844, ECO:0007744|PDB:1AGY

Chain	Residue	Details
A	ASP175

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site_id	SWS_FT_FI3
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:1560844, ECO:0007744|PDB:1AGY

Chain	Residue	Details
A	HIS188

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site_id	SWS_FT_FI4
Number of Residues	1
Details	SITE: Transition state stabilizer => ECO:0000269|PubMed:1560844, ECO:0000269|PubMed:8286366, ECO:0000269|PubMed:8555209, ECO:0000269|PubMed:9041628, ECO:0007744|PDB:1AGY, ECO:0007744|PDB:1FFE, ECO:0007744|PDB:1OXM, ECO:0007744|PDB:2CUT

Chain	Residue	Details
A	SER42

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site_id	SWS_FT_FI5
Number of Residues	1
Details	SITE: Transition state stabilizer => ECO:0000269|PubMed:1560844, ECO:0000269|PubMed:8286366, ECO:0000269|PubMed:9041628, ECO:0007744|PDB:1AGY, ECO:0007744|PDB:1OXM, ECO:0007744|PDB:2CUT

Chain	Residue	Details
A	GLN121

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: N-D-glucuronoyl glycine => ECO:0000269|PubMed:7398618

Chain	Residue	Details
A	GLU16

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Catalytic Information from CSA

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

Chain	Residue	Details
A	ASP175
A	GLN121
A	SER42
A	SER120
A	HIS188

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site_id	MCSA1
Number of Residues	5
Details	M-CSA 631

Chain	Residue	Details
A	SER42	electrostatic stabiliser
A	SER120	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
A	GLN121	electrostatic stabiliser
A	ASP175	electrostatic stabiliser, increase basicity
A	HIS188	proton acceptor, proton donor

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