2AVV

Kinetics, stability, and structural changes in high resolution crystal structures of HIV-1 protease with drug resistant mutations L24I, I50V, and G73S

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
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL D 501

Chain	Residue
D	GLU21
D	HOH1234

---

site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL B 502

Chain	Residue
B	SER37

---

site_id	AC3
Number of Residues	34
Details	BINDING SITE FOR RESIDUE MK1 A 901

Chain	Residue
A	ASP30
A	GLY48
A	GLY49
A	ILE50
A	VAL82
A	ILE84
A	HOH1008
A	HOH1142
A	HOH1203
A	HOH1280
A	HOH1318
A	HOH1319
A	HOH1329
B	ARG8
B	LEU23
B	ASP25
B	GLY27
B	ALA28
B	ASP29
B	ASP30
B	VAL32
B	GLY48
B	GLY49
B	ILE50
B	PRO81
B	VAL82
B	ILE84
B	HOH1281
A	ARG8
A	LEU23
A	ASP25
A	GLY27
A	ALA28
A	ASP29

---

site_id	AC4
Number of Residues	33
Details	BINDING SITE FOR RESIDUE MK1 E 902

Chain	Residue
D	ARG8
D	LEU23
D	ASP25
D	GLY27
D	ASP29
D	ASP30
D	VAL32
D	GLY48
D	GLY49
D	ILE50
D	PRO81
D	VAL82
D	ILE84
D	HOH1258
D	HOH1362
E	LEU23
E	ASP25
E	GLY27
E	ALA28
E	ASP29
E	ASP30
E	VAL32
E	GLY48
E	GLY49
E	ILE50
E	PRO81
E	VAL82
E	ILE84
E	HOH1039
E	HOH1128
E	HOH1215
E	HOH1320
E	HOH1338

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACY A 601

Chain	Residue
A	MET36
A	SER37
A	HOH1174
B	PRO39
B	GLY40

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACY B 602

Chain	Residue
B	THR12
B	GLU65
B	ALA67
B	GLY68
D	LYS55

---

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACY E 603

Chain	Residue
B	LYS7
D	PRO39
D	GLY40
D	HOH1135
E	MET36
E	SER37
E	HOH1358

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ALA22-ILE33

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	276
Details	Domain: {"description":"Peptidase A2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00275","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	40
Details	Region: {"description":"Dimerization of protease","evidences":[{"source":"UniProtKB","id":"P04585","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Active site: {"description":"For protease activity; shared with dimeric partner","evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1a30

Chain	Residue	Details
A	ASP25
A	THR26
B	ASP25
B	THR26

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1a30

Chain	Residue	Details
D	ASP25
D	THR26
E	ASP25
E	THR26

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1a30

Chain	Residue	Details
A	ASP25
B	ASP25

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1a30

Chain	Residue	Details
D	ASP25
E	ASP25

---