2B7F

Crystal structure of human T-cell leukemia virus protease, a novel target for anti-cancer design

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004190	molecular_function	aspartic-type endopeptidase activity
A	0006508	biological_process	proteolysis
B	0004190	molecular_function	aspartic-type endopeptidase activity
B	0006508	biological_process	proteolysis
C	0004190	molecular_function	aspartic-type endopeptidase activity
C	0006508	biological_process	proteolysis
D	0004190	molecular_function	aspartic-type endopeptidase activity
D	0006508	biological_process	proteolysis
E	0004190	molecular_function	aspartic-type endopeptidase activity
E	0006508	biological_process	proteolysis
F	0004190	molecular_function	aspartic-type endopeptidase activity
F	0006508	biological_process	proteolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 A 201

Chain	Residue
A	TYR114
A	LEU115
A	PRO116
B	PRO1
E	TYR114
E	LEU115
E	PRO116
F	PRO1

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 C 202

Chain	Residue
C	LEU115
C	LEU115
C	PRO116
C	PRO116
D	PRO1
D	ARG81
C	TYR114

---

site_id	AC3
Number of Residues	22
Details	BINDING SITE FOR CHAIN I OF (ACE)APQV(STA)VMHP PEPTIDE

Chain	Residue
A	ARG10
A	ASP32
A	GLY34
A	ALA35
A	ASP36
A	MET37
A	SER55
A	VAL56
A	LEU57
A	GLN62
A	TRP98
B	ARG10
B	ASP32
B	GLY34
B	ALA35
B	ASP36
B	SER55
B	LEU57
B	GLY58
B	ALA59
B	TRP98
I	HOH1

---

site_id	AC4
Number of Residues	24
Details	BINDING SITE FOR CHAIN J OF (ACE)APQV(STA)VMHP PEPTIDE

Chain	Residue
C	ARG10
C	ASP32
C	GLY34
C	ALA35
C	ASP36
C	SER55
C	VAL56
C	LEU57
C	GLY58
C	ALA59
C	TRP98
C	ILE100
D	ARG10
D	ASP32
D	GLY34
D	ALA35
D	ASP36
D	MET37
D	SER55
D	VAL56
D	LEU57
D	GLY58
D	TRP98
D	HOH117

---

site_id	AC5
Number of Residues	20
Details	BINDING SITE FOR CHAIN K OF (ACE)APQV(STA)VMHP PEPTIDE

Chain	Residue
E	ARG10
E	ASP32
E	GLY34
E	ALA35
E	ASP36
E	MET37
E	SER55
E	LEU57
E	GLN62
E	TRP98
F	ARG10
F	ASP32
F	GLY34
F	ALA35
F	ASP36
F	SER55
F	LEU57
F	ALA59
F	TRP98
K	HOH3

---

Functional Information from PROSITE/UniProt

site_id	PS00141
Number of Residues	12
Details	ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADMTVI

Chain	Residue	Details
A	ALA29-ILE40

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	SITE: Cleavage; by viral protease => ECO:0000269|PubMed:10037763

Chain	Residue	Details
A	TRP98
B	TRP98
C	TRP98
D	TRP98
E	TRP98
F	TRP98

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	MOD_RES: Phosphoserine; by host MAPK1 => ECO:0000250|UniProtKB:P03345

Chain	Residue	Details
A	PRO73
B	PRO73
C	PRO73
D	PRO73
E	PRO73
F	PRO73

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	ACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094

Chain	Residue	Details
A	ASP32
B	ASP32
C	ASP32
D	ASP32
E	ASP32
F	ASP32

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