Structure of PDB 4l8w Chain I Binding Site BS01

Receptor Information
>4l8w Chain I (length=287) Species: 7955 (Danio rerio) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KTNERPIIGVLAQDVFDPKPDRNSYIAASYVKFLESAGARVVPVMINKSE
DEYSRLFKSINGVLFPGGGVSLESSGYSKAAGIFYRLALEANSNGDYFPV
WGTCLGFELLTLLTSGELLLSHTNTSGIALPLDFTEDVKGSRLFKEFPEE
LMKSLATEPLTENSHQWSITTENFTANKKLKKFYRVLSTNTDGYNKFVST
MEAYDFPIYATQWNPEKNAFEWTRPYIPHTPSAIKTTFYMANFFVNEARK
NLHSFASTEEEEKALIYNYKPEYTGIQSAFEQTYFFN
Ligand information
Ligand IDMTX
InChIInChI=1S/C20H22N8O5/c1-28(9-11-8-23-17-15(24-11)16(21)26-20(22)27-17)12-4-2-10(3-5-12)18(31)25-13(19(32)33)6-7-14(29)30/h2-5,8,13H,6-7,9H2,1H3,(H,25,31)(H,29,30)(H,32,33)(H4,21,22,23,26,27)/t13-/m0/s1
InChIKeyFBOZXECLQNJBKD-ZDUSSCGKSA-N
SMILES
SoftwareSMILES
CACTVS 3.341CN(Cc1cnc2nc(N)nc(N)c2n1)c3ccc(cc3)C(=O)N[CH](CCC(O)=O)C(O)=O
CACTVS 3.341CN(Cc1cnc2nc(N)nc(N)c2n1)c3ccc(cc3)C(=O)N[C@@H](CCC(O)=O)C(O)=O
OpenEye OEToolkits 1.5.0CN(Cc1cnc2c(n1)c(nc(n2)N)N)c3ccc(cc3)C(=O)NC(CCC(=O)O)C(=O)O
ACDLabs 10.04O=C(O)C(NC(=O)c1ccc(cc1)N(C)Cc2nc3c(nc2)nc(nc3N)N)CCC(=O)O
OpenEye OEToolkits 1.5.0CN(Cc1cnc2c(n1)c(nc(n2)N)N)c3ccc(cc3)C(=O)N[C@@H](CCC(=O)O)C(=O)O
FormulaC20 H22 N8 O5
NameMETHOTREXATE
ChEMBLCHEMBL34259
DrugBankDB00563
ZINCZINC000001529323
PDB chain4l8w Chain I Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4l8w Structural insights into the hydrolysis and polymorphism of methotrexate polyglutamate by zebrafish gamma-glutamyl hydrolase
Resolution2.39 Å
Binding residue
(original residue number in PDB)		F20 G72 G73 C108 L109 E112 H169 Q170 W171
Binding residue
(residue number reindexed from 1)		F16 G68 G69 C104 L105 E108 H165 Q166 W167
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) E220
Catalytic site (residue number reindexed from 1) E216
Enzyme Commision number 3.4.19.9: folate gamma-glutamyl hydrolase.
Gene Ontology
Molecular Function
GO:0008242 omega peptidase activity
GO:0016787 hydrolase activity

View graph for
Molecular Function
External links
PDB RCSB:4l8w, PDBe:4l8w, PDBj:4l8w
PDBsum4l8w
PubMed24028568
UniProtQ6NY42

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