Structure of PDB 4bbh Chain B

Receptor sequence

>4bbhB (length=384) Species: 5855 (Plasmodium vivax) [Search protein sequence]

DYKFWYTQPVPKINDEFNESVNEPFISDNKVEDVRKDEYKLPPGYSWYVC
DVKDEKDRSEIYTLLTDNYVEDDDNIFRFNYSAEFLLWALTSPNYLKTWH
IGVKYDASNKLIGFISAIPTDICIHKRTIKMAEVNFLCVHKTLRSKRLAP
VLIKEITRRINLENIWQAIYTAGVYLPKPVSDARYYHRSINVKKLIEIGF
SSLNSRLTMSRAIKLYRVEDTLNIKNMRLMKKKDVEGVHKLLGSYLEQFN
LYAVFTKEEIAHWFLPIENVIYTYVNEENGKIKDMISFYSLPSQILGNDK
YSTLNAAYSFYNVTTTATFKQLMQDAILLAKRNNFDVFNALEVMQNKSVF
EDLKFGEGDGSLKYYLYNWKCASFAPAHVGIVLL

3D structure

PDB

4bbh Discovery of Novel and Ligand-Efficient Inhibitors of Plasmodium Falciparum and Plasmodium Vivax N-Myristoyltransferase.

Chain

Resolution

1.63 Å

3D
structure

Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]

Enzymatic activity

Catalytic site (original residue number in PDB)	N161 F162 L163 T197 L410
Catalytic site (residue number reindexed from 1)	N135 F136 L137 T171 L384
Enzyme Commision number	2.3.1.97: glycylpeptide N-tetradecanoyltransferase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	NHW	B	Y28 F30 W31 Y95 V96 N161 L163 C164 V165 R170 S171 R173 L174 A175 P176 T183 I186 W192 A194 Y196 T197 L202 Y393	Y2 F4 W5 Y69 V70 N135 L137 C138 V139 R144 S145 R147 L148 A149 P150 T157 I160 W166 A168 Y170 T171 L176 Y367
BS02	YBN	B	V96 Y211 Y315 Y334 N365 A366 L367 L388 L409 L410	V70 Y185 Y289 Y308 N339 A340 L341 L362 L383 L384	MOAD: Ki=0.08uM
BS03	MG	B	L169 K172 L174	L143 K146 L148

Gene Ontology

	Molecular Function
GO:0004379	glycylpeptide N-tetradecanoyltransferase activity
GO:0016746	acyltransferase activity
GO:0046872	metal ion binding

	Biological Process
GO:0006499	N-terminal protein myristoylation
GO:0018008	N-terminal peptidyl-glycine N-myristoylation

	Cellular Component
GO:0005737	cytoplasm

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:4bbh, PDBe:4bbh, PDBj:4bbh
PDBsum	4bbh
PubMed	23170970
UniProt	A5K1A2

[Back to BioLiP]