Structure of PDB 1j2b Chain B

Receptor sequence

>1j2bB (length=576) Species: 53953 (Pyrococcus horikoshii) [Search protein sequence]

MLKFEIKARDGAGRIGKLEVNGKKIETPAIMPVVNPKQMVVEPKELEKMG
FEIIITNSYIIYKDEELRRKALELGIHRMLDYNGIIEVDSGSFQLMKYGS
IEVSNREIIEFQHRIGVDIGTFLDIPTPPDAPREQAVKELEITLSRAREA
EEIKEIPMNATIQGSTYTDLRRYAARRLSSMNFEIHPIGGVVPLLESYRF
RDVVDIVISSKMALRPDRPVHLFGAGHPIVFALAVAMGVDLFDSASYALY
AKDDRYMTPEGTKRLDELDYFPCSCPVCSKYTPQELREMPKEERTRLLAL
HNLWVIKEEIKRVKQAIKEGELWRLVDERARSHPKLYSAYKRLLEHYTFL
EEFEPITKKSALFKISNESLRWPVVRRAKERAKSINERFGELVEHPIFGR
VSRYLSLTYPFAQSEAEDDFKIEKPTKEDAIKYVMAIAEYQFGEGASRAF
DDAKVELSKTGMPRQVKVNGKRLATVRADDGLLTLGIEGAKRLHRVLPYP
RMRVVVNKEAEPFARKGKDVFAKFVIFADPGIRPYDEVLVVNENDELLAT
GQALLSGREMIVFQYGRAVKVRKGVE

3D structure

PDB

1j2b Alternative Tertiary Structure of tRNA for Recognition by a Posttranscriptional Modification Enzyme

Chain

Resolution

3.3 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	D249 C279 C281 C284 H307
Catalytic site (residue number reindexed from 1)	D243 C273 C275 C278 H301
Enzyme Commision number	2.4.2.48: tRNA-guanine(15) transglycosylase.

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)
BS01	rna	B	V39 N41 K43 Q44 I66 D95 S98 F99 Q100 K103 Y104 D130 P132 D136 G195 V198 L201 E202 Y204 R205 R207 F229 G230 A231 G232 H233 D249 S250 A251 L255 Y256 K258 R261 T268 H339	V33 N35 K37 Q38 I60 D89 S92 F93 Q94 K97 Y98 D124 P126 D130 G189 V192 L195 E196 Y198 R199 R201 F223 G224 A225 G226 H227 D243 S244 A245 L249 Y250 K252 R255 T262 H333
BS02	rna	B	A367 A418 D424 D425 K427 I428 S464 K465 T466 M468 Q471 R478 T481 A484 F519 F527 F530	A361 A412 D418 D419 K421 I422 S458 K459 T460 M462 Q465 R472 T475 A478 F513 F521 F524
BS03	ZN	B	C279 C284 H307	C273 C278 H301
BS04	MG	B	A528 I567	A522 I561

Gene Ontology

	Molecular Function
GO:0003723	RNA binding
GO:0008270	zinc ion binding
GO:0016757	glycosyltransferase activity
GO:0016763	pentosyltransferase activity
GO:0046872	metal ion binding

	Biological Process
GO:0002099	tRNA wobble guanine modification
GO:0006400	tRNA modification
GO:0008033	tRNA processing
GO:0008616	queuosine biosynthetic process

	Cellular Component
GO:0005737	cytoplasm

View graph for
Molecular Function

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Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:1j2b, PDBe:1j2b, PDBj:1j2b
PDBsum	1j2b
PubMed	12732145
UniProt	O58843\|ATGT_PYRHO tRNA-guanine(15) transglycosylase (Gene Name=tgtA)

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