Structure of PDB 2hqp Chain A

Receptor sequence
>2hqpA (length=162) Species: 1582 (Lacticaseibacillus casei) [Search protein sequence]
TAFLWAQDRDGLIGKDGHLPWHLPDDLHYFRAQTVGKIMVVGRRTYESFP
KRPLPERTNVVLTHQEDYQAQGAVVVHDVAAVFAYAKQHPDQELVIAGGA
QIFTAFKDDVDTLLVTRLAGSFEGDTKMIPLNWDDFTKVSSRTVEDTNPA
LTHTYEVWQKKA
3D structure
PDB2hqp Structural insights into cooperative effects of ligand binding to L. casei dihydrofolate redutase
ChainA
ResolutionN/A
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L4 L19 W21 D26 L27 F30 L54 L94 T116
Catalytic site (residue number reindexed from 1) L4 L19 W21 D26 L27 F30 L54 L94 T116
Enzyme Commision number 1.5.1.3: dihydrofolate reductase.
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 NDP A W5 A6 I13 R43 R44 T45 L62 T63 H64 H77 V79 G98 G99 A100 Q101 I102 W5 A6 I13 R43 R44 T45 L62 T63 H64 H77 V79 G98 G99 A100 Q101 I102
Gene Ontology
Molecular Function
GO:0004146 dihydrofolate reductase activity
GO:0016491 oxidoreductase activity
GO:0050661 NADP binding
Biological Process
GO:0006730 one-carbon metabolic process
GO:0031427 response to methotrexate
GO:0046452 dihydrofolate metabolic process
GO:0046654 tetrahydrofolate biosynthetic process
GO:0046655 folic acid metabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0005829 cytosol

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External links
PDB RCSB:2hqp, PDBe:2hqp, PDBj:2hqp
PDBsum2hqp
PubMed
UniProtP00381|DYR_LACCA Dihydrofolate reductase (Gene Name=folA)

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