1KJ4

SUBSTRATE SHAPE DETERMINES SPECIFICITY OF RECOGNITION RECOGNITION FOR HIV-1 PROTEASE: ANALYSIS OF CRYSTAL STRUCTURES OF SIX SUBSTRATE COMPLEXES

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE ACT B 501

Chain	Residue
B	HIS69

---

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACT B 502

Chain	Residue
B	TRP6
B	LYS7

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACT A 504

Chain	Residue
A	LYS7
A	ARG8

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT A 506

Chain	Residue
A	GLY73
A	THR74
A	ASN88

---

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACT A 512

Chain	Residue
D	HIS69
A	ARG14

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT C 516

Chain	Residue
B	GLY17
C	GLY73
C	THR74
C	ASN88
C	GLN92

---

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACT D 518

Chain	Residue
D	ARG14
D	GLY17

---

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT B 522

Chain	Residue
B	ARG8
D	ARG8
D	LEU10

---

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT D 523

Chain	Residue
C	ACT524
D	ARG8
S	VAL1

---

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT C 524

Chain	Residue
C	ARG87
D	TRP6
D	ACT523

---

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

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Site: {"description":"Cleavage; by viral protease","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine; by host","evidences":[{"evidenceCode":"ECO:0000250"}]}

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	ASN25
A	THR26
B	ASN25
B	THR26

---

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

Chain	Residue	Details
D	ASN25
D	THR26
C	ASN25
C	THR26

---

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

Chain	Residue	Details
A	ASN25
B	ASN25

---

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

Chain	Residue	Details
C	ASN25
D	ASN25

---