1KYZ

Crystal Structure Analysis of Caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase Ferulic Acid Complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008168	molecular_function	methyltransferase activity
A	0008171	molecular_function	O-methyltransferase activity
A	0008757	molecular_function	S-adenosylmethionine-dependent methyltransferase activity
A	0009699	biological_process	phenylpropanoid biosynthetic process
A	0009809	biological_process	lignin biosynthetic process
A	0019438	biological_process	obsolete aromatic compound biosynthetic process
A	0032259	biological_process	methylation
A	0046983	molecular_function	protein dimerization activity
A	0047763	molecular_function	caffeate O-methyltransferase activity
C	0008168	molecular_function	methyltransferase activity
C	0008171	molecular_function	O-methyltransferase activity
C	0008757	molecular_function	S-adenosylmethionine-dependent methyltransferase activity
C	0009699	biological_process	phenylpropanoid biosynthetic process
C	0009809	biological_process	lignin biosynthetic process
C	0019438	biological_process	obsolete aromatic compound biosynthetic process
C	0032259	biological_process	methylation
C	0046983	molecular_function	protein dimerization activity
C	0047763	molecular_function	caffeate O-methyltransferase activity
E	0008168	molecular_function	methyltransferase activity
E	0008171	molecular_function	O-methyltransferase activity
E	0008757	molecular_function	S-adenosylmethionine-dependent methyltransferase activity
E	0009699	biological_process	phenylpropanoid biosynthetic process
E	0009809	biological_process	lignin biosynthetic process
E	0019438	biological_process	obsolete aromatic compound biosynthetic process
E	0032259	biological_process	methylation
E	0046983	molecular_function	protein dimerization activity
E	0047763	molecular_function	caffeate O-methyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE SAH E 1697

Chain	Residue
E	GLY208
E	TRP266
E	TRP271
E	HOH1749
E	HOH1771
E	ASP231
E	LEU232
E	VAL235
E	ASP251
E	MET252
E	PHE253
E	MET264
E	LYS265

---

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FER E 1698

Chain	Residue
E	MET130
E	ASN131
E	LEU136
E	ALA162
E	PHE176
E	ASP270
E	ILE316
E	MET320
E	HOH1814

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FER C 366

Chain	Residue
C	MET130
C	ASN131
C	LEU136
C	ALA162
C	HIS166
C	MET320

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FER A 366

Chain	Residue
A	ASN131
A	ALA162
A	PHE176

---

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE SAH A 1698

Chain	Residue
A	SER184
A	GLY208
A	GLY210
A	ASP231
A	LEU232
A	VAL235
A	ASP251
A	MET252
A	PHE253
A	MET264
A	LYS265
A	ILE267
A	TRP271

---

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SAH C 1699

Chain	Residue
C	GLY208
C	ASP231
C	LEU232
C	VAL235
C	ASP251
C	MET252
C	PHE253
C	MET264
C	LYS265
C	TRP266
C	TRP271

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01020, ECO:0000305|PubMed:12084826

Chain	Residue	Details
A	HIS269
C	HIS269
E	HIS269

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:F1DBB3

Chain	Residue	Details
A	GLU297
A	GLU329
C	GLU297
C	GLU329
E	GLU297
E	GLU329

---

site_id	SWS_FT_FI3
Number of Residues	21
Details	BINDING: BINDING => ECO:0000269|PubMed:12084826, ECO:0007744|PDB:1KYZ

Chain	Residue	Details
A	ASP251
A	MET252
A	MET264
A	LYS265
C	ASN131
C	GLY208
C	ASP231
C	ASP251
C	MET252
C	MET264
C	LYS265
E	ASN131
E	GLY208
E	ASP231
E	ASP251
E	MET252
E	MET264
E	LYS265
A	ASN131
A	GLY208
A	ASP231

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:12084826, ECO:0007744|PDB:1KYW

Chain	Residue	Details
A	ASP270
C	ASP270
E	ASP270

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 621

Chain	Residue	Details
A	HIS269	proton acceptor, proton donor
A	ASP270	electrostatic stabiliser, steric role
A	GLU297	electrostatic stabiliser, steric role
A	GLU329	electrostatic stabiliser, hydrogen bond donor, steric role

---

site_id	MCSA2
Number of Residues	4
Details	M-CSA 621

Chain	Residue	Details
C	HIS269	proton acceptor, proton donor
C	ASP270	electrostatic stabiliser, steric role
C	GLU297	electrostatic stabiliser, steric role
C	GLU329	electrostatic stabiliser, hydrogen bond donor, steric role

---

site_id	MCSA3
Number of Residues	4
Details	M-CSA 621

Chain	Residue	Details
E	HIS269	proton acceptor, proton donor
E	ASP270	electrostatic stabiliser, steric role
E	GLU297	electrostatic stabiliser, steric role
E	GLU329	electrostatic stabiliser, hydrogen bond donor, steric role

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