Structure of PDB 5nna Chain B Binding Site BS01

Receptor Information

>5nna Chain B (length=256) Species: 187304 (Roseibium aggregatum) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

SSLNQLVSGLASGAVRIVDLTHTLDPDFPVIVLPPEFGQCARFRMEEISA
YDHRGPAWKWHNISMSEHTGTHFDAPSHWISGKDVPNGSVDEIPAEAFVG
PVVVIDCSKGAAENDDFELTPEIIAGWESEHGRIPEDAWVLMRTDWSKRR
GADYLNMRADGPHSPGPTPEAIRFLIEERNIRGFGTETVGTDAGQGAHYV
PPYPAHYLLHGAGKYGLQCLANLDQLPATGAVLIAAPLKIKNGTGSPLRV
LAMVTE

Ligand information

Ligand ID

BZM

InChI

InChI=1S/C14H12O2/c15-14(13-9-5-2-6-10-13)16-11-12-7-3-1-4-8-12/h1-10H,11H2

InChIKey

SESFRYSPDFLNCH-UHFFFAOYSA-N

SMILES

Software	SMILES
OpenEye OEToolkits 1.5.0	c1ccc(cc1)COC(=O)c2ccccc2
ACDLabs 10.04 CACTVS 3.341	O=C(OCc1ccccc1)c2ccccc2

Formula

C14 H12 O2

Name

BENZOIC ACID PHENYLMETHYLESTER

PDB chain

5nna Chain B Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	5nna A fundamental catalytic difference between zinc and manganese dependent enzymes revealed in a bacterial isatin hydrolase.
Resolution	1.5 Å
Binding residue (original residue number in PDB)	I32 L34 W80 P163 V190 G191 G195 Y204 H207
Binding residue (residue number reindexed from 1)	I31 L33 W79 P162 V189 G190 G194 Y203 H206
Annotation score	1

Enzymatic activity

Enzyme Commision number

Gene Ontology

	Molecular Function
GO:0004061	arylformamidase activity
GO:0046872	metal ion binding

	Biological Process
GO:0019441	tryptophan catabolic process to kynurenine

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Molecular Function

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Biological Process

External links

PDB	RCSB:5nna, PDBe:5nna, PDBj:5nna
PDBsum	5nna
PubMed	30166577
UniProt	A0P0F0

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