Structure of PDB 7k6c Chain B

Receptor sequence
>7k6cB (length=160) Species: 561007 (Mycobacteroides abscessus ATCC 19977) [Search protein sequence]
GTIGLIWAQTRAGVIGADGAIPWRLPEDQARFKRITMGHTVIMGRKTWES
LPGSVRPLPGRPNIVLTRDALFEPDGALAVGSADAALAASDEAPWVIGGG
EIYRLFLPLAQRCEVTVVEADVPGDALAPELGEGWVVETNDWQTSESGLR
YQFLSYRKVD
3D structure
PDB7k6c Crystal Structure of Dihydrofolate reductase (DHFR) from Mycobacterium abscessus ATCC 19977 / DSM 44196 with NADP and inhibitor P218
ChainB
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) I8 I23 W25 D30 Q31 F34 L60 P96 T118
Catalytic site (residue number reindexed from 1) I6 I21 W23 D28 Q29 F32 L58 P94 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 NAP B W9 A10 I17 G18 G21 A22 G46 R47 K48 T49 L68 T69 R70 G83 I99 G101 G102 E103 I104 W7 A8 I15 G16 G19 A20 G44 R45 K46 T47 L66 T67 R68 G81 I97 G99 G100 E101 I102
BS02 MMV B I8 W9 D30 Q31 F34 L53 L60 R63 I99 I6 W7 D28 Q29 F32 L51 L58 R61 I97
BS03 CA B G55 R58 G53 R56
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004146 dihydrofolate reductase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
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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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:7k6c, PDBe:7k6c, PDBj:7k6c
PDBsum7k6c
PubMed
UniProtB1MD46

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