Structure of PDB 2zza Chain A

Receptor sequence
>2zzaA (length=161) Species: 111291 (Moritella profunda) [Search protein sequence]
VIVSMIAALANNRVIGLDNKMPWHLPAELQLFKRATLGKPIVMGRNTFES
IGRPLPGRLNIVLSRQTDYQPEGVTVVATLEDAVVAAGDVEELMIIGGAT
IYNQCLAAADRLYLTHIELTTEGDTWFPDYEQYNWQEIEHESYAADDKNP
HNYRFSLLERV
3D structure
PDB2zza Moritella profunda Dihydrofolate reductase complex with NADP+ and Folate
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) I6 M21 W23 E28 L29 F32 L55 L93 T115
Catalytic site (residue number reindexed from 1) I6 M21 W23 E28 L29 F32 L55 L93 T115
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 NAP A A7 A8 I15 N19 K20 M21 G44 R45 N46 T47 L63 S64 R65 A78 I96 G98 A99 T100 I101 Y102 Q104 A7 A8 I15 N19 K20 M21 G44 R45 N46 T47 L63 S64 R65 A78 I96 G98 A99 T100 I101 Y102 Q104
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004146 dihydrofolate reductase activity
GO:0016491 oxidoreductase activity
GO:0050661 NADP binding
Biological Process
GO:0006730 one-carbon metabolic process
GO:0046452 dihydrofolate metabolic process
GO:0046654 tetrahydrofolate biosynthetic process
GO:0046655 folic acid metabolic process
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:2zza, PDBe:2zza, PDBj:2zza
PDBsum2zza
PubMed
UniProtQ70YQ6

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