1OXM

STRUCTURE OF CUTINASE

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TC4 A 901

Chain	Residue
A	SER120
A	GLN121
A	VAL184
A	HIS188
A	LEU189
B	VAL184
B	HOH664
B	TC4901
A	SER42
A	THR43
A	TYR119

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site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TC4 B 901

Chain	Residue
A	LEU189
A	HOH712
A	TC4901
B	SER42
B	THR43
B	LEU81
B	SER120
B	GLN121
B	VAL184
B	HIS188
B	LEU189

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site_id	TC4
Number of Residues	6
Details	CATALYTIC TRIAD

Chain	Residue
A	SER120
B	SER120
A	HIS188
B	HIS188
A	ASP175
B	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	2
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:1560844, ECO:0007744|PDB:1AGY

Chain	Residue	Details
A	SER120
B	SER120

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000269|PubMed:1560844, ECO:0007744|PDB:1AGY

Chain	Residue	Details
A	ASP175
B	ASP175

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site_id	SWS_FT_FI3
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:1560844, ECO:0007744|PDB:1AGY

Chain	Residue	Details
A	HIS188
B	HIS188

---

site_id	SWS_FT_FI4
Number of Residues	2
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
B	SER42

---

site_id	SWS_FT_FI5
Number of Residues	2
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
B	GLN121

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: N-D-glucuronoyl glycine => ECO:0000269|PubMed:7398618

Chain	Residue	Details
A	GLY16
B	GLY16

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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

---

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

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

---

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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site_id	MCSA2
Number of Residues	5
Details	M-CSA 631

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

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