4STD

HIGH RESOLUTION STRUCTURES OF SCYTALONE DEHYDRATASE-INHIBITOR COMPLEXES CRYSTALLIZED AT PHYSIOLOGICAL PH

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005575	cellular_component	cellular_component
A	0005768	cellular_component	endosome
A	0006582	biological_process	melanin metabolic process
A	0016829	molecular_function	lyase activity
A	0030411	molecular_function	scytalone dehydratase activity
A	0042438	biological_process	melanin biosynthetic process
A	0046872	molecular_function	metal ion binding
B	0005575	cellular_component	cellular_component
B	0005768	cellular_component	endosome
B	0006582	biological_process	melanin metabolic process
B	0016829	molecular_function	lyase activity
B	0030411	molecular_function	scytalone dehydratase activity
B	0042438	biological_process	melanin biosynthetic process
B	0046872	molecular_function	metal ion binding
C	0005575	cellular_component	cellular_component
C	0005768	cellular_component	endosome
C	0006582	biological_process	melanin metabolic process
C	0016829	molecular_function	lyase activity
C	0030411	molecular_function	scytalone dehydratase activity
C	0042438	biological_process	melanin biosynthetic process
C	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE BFS A 173

Chain	Residue
A	TYR30
A	LEU147
A	PRO149
A	ILE151
A	PHE158
A	PHE162
A	GLY165
A	HOH187
A	HOH190
A	TYR50
A	VAL75
A	LEU76
A	LEU106
A	HIS110
A	ALA127
A	SER129
A	ASN131

---

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE BFS B 174

Chain	Residue
B	TYR30
B	TYR50
B	VAL108
B	HIS110
B	ALA127
B	SER129
B	ASN131
B	LEU147
B	PRO149
B	PHE158
B	PHE162
B	HOH189

---

site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE BFS C 175

Chain	Residue
C	TYR30
C	TYR50
C	PHE53
C	LEU76
C	LEU106
C	VAL108
C	HIS110
C	ALA127
C	SER129
C	ASN131
C	LEU147
C	PHE158
C	GLY165
C	HOH185
C	HOH188

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: ACT_SITE => ECO:0000305|PubMed:7866745

Chain	Residue	Details
A	HIS85
A	HIS110
B	HIS85
B	HIS110
C	HIS85
C	HIS110

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000305|PubMed:9922139

Chain	Residue	Details
A	TYR30
B	TYR30
C	TYR30

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000305|PubMed:9665698

Chain	Residue	Details
A	TYR50
B	TYR50
C	TYR50

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0000305|PubMed:10382670

Chain	Residue	Details
A	PHE53
B	PHE53
C	PHE53

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	BINDING: BINDING => ECO:0000305|PubMed:10382670, ECO:0000305|PubMed:7866745, ECO:0000305|PubMed:9922139

Chain	Residue	Details
A	ASN131
B	ASN131
C	ASN131

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 910

Chain	Residue	Details
A	TYR30	modifies pKa
A	ASP31	modifies pKa
A	TYR50	proton acceptor, proton donor
A	HIS85	proton acceptor, proton donor
A	HIS110	electrostatic stabiliser

---

site_id	MCSA2
Number of Residues	5
Details	M-CSA 910

Chain	Residue	Details
B	TYR30	modifies pKa
B	ASP31	modifies pKa
B	TYR50	proton acceptor, proton donor
B	HIS85	proton acceptor, proton donor
B	HIS110	electrostatic stabiliser

---

site_id	MCSA3
Number of Residues	5
Details	M-CSA 910

Chain	Residue	Details
C	TYR30	modifies pKa
C	ASP31	modifies pKa
C	TYR50	proton acceptor, proton donor
C	HIS85	proton acceptor, proton donor
C	HIS110	electrostatic stabiliser

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