1LWF

CRYSTAL STRUCTURE OF A MUTANT HIV-1 REVERSE TRANSCRIPTASE (RTMQ+M184V: M41L/D67N/K70R/M184V/T215Y) IN COMPLEX WITH NEVIRAPINE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003676	molecular_function	nucleic acid binding
A	0003964	molecular_function	RNA-directed DNA polymerase activity
A	0004523	molecular_function	RNA-DNA hybrid ribonuclease activity
A	0006278	biological_process	RNA-templated DNA biosynthetic process
B	0003964	molecular_function	RNA-directed DNA polymerase activity
B	0006278	biological_process	RNA-templated DNA biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE NVP A 999

Chain	Residue
A	LEU100
A	TYR318
A	LYS101
A	TYR181
A	TYR188
A	GLY190
A	PHE227
A	TRP229
A	LEU234
A	HIS235

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	17
Details	ZN_FING: CCHC-type 1 => ECO:0000255|PROSITE-ProRule:PRU00047

Chain	Residue	Details
B	HIS235-TRP252

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site_id	SWS_FT_FI2
Number of Residues	17
Details	ZN_FING: CCHC-type 2 => ECO:0000255|PROSITE-ProRule:PRU00047

Chain	Residue	Details
B	ASP256-GLY273

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site_id	SWS_FT_FI3
Number of Residues	1
Details	ACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000305|PubMed:33542150

Chain	Residue	Details
B	ARG358

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site_id	SWS_FT_FI4
Number of Residues	1
Details	SITE: Cis/trans isomerization of proline peptide bond; by human PPIA/CYPA

Chain	Residue	Details
B	LYS66

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site_id	SWS_FT_FI5
Number of Residues	4
Details	SITE: Cleavage; by viral protease => ECO:0000250

Chain	Residue	Details
B	HIS208
B	GLN222
B	GLY285
B	GLU432

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site_id	SWS_FT_FI6
Number of Residues	3
Details	SITE: Cleavage; by viral protease => ECO:0000255

Chain	Residue	Details
B	LYS238
B	TYR271
B	ARG277
A	GLU432

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site_id	SWS_FT_FI7
Number of Residues	1
Details	SITE: Cleavage; by viral protease => ECO:0000305|PubMed:15183348

Chain	Residue	Details
B	GLY333
A	TYR271
A	ARG277

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site_id	SWS_FT_FI8
Number of Residues	1
Details	SITE: Cleavage; by viral protease => ECO:0000305|PubMed:15183348

Chain	Residue	Details
A	GLY333

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 175

Chain	Residue	Details
B	ARG358	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	GLY359	electrostatic stabiliser, transition state stabiliser
B	ALA360	electrostatic stabiliser, hydrogen bond donor

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