Structure of PDB 1drv Chain A Binding Site BS01
Receptor Information
>1drv Chain A (length=270) Species:
562
(Escherichia coli) [
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ANIRVAIAGAGGRMGRQLIQAALALEGVQLGAALEREGSSLLGSDAGELA
GAGKTGVTVQSSLDAVKDDFDVFIDFTRPEGTLNHLAFCRQHGKGMVIGT
TGFDEAGKQAIRDAAADIAIVFAANFSVGVNVMLKLLEKAAKVMGDYTDI
EIIEAHHRHKVDAPSGTALAMGEAIAHALDKDLKDCAVYSREGHTGERVP
GTIGFATVRAGDIVGEHTAMFADIGERLEITHKASSRMTFANGAVRSALW
LSGKESGLFDMRDVLDLNNL
Ligand information
Ligand ID
A3D
InChI
InChI=1S/C22H28N6O14P2/c1-10(29)11-3-2-4-27(5-11)21-17(32)15(30)12(40-21)6-38-43(34,35)42-44(36,37)39-7-13-16(31)18(33)22(41-13)28-9-26-14-19(23)24-8-25-20(14)28/h2-5,8-9,12-13,15-18,21-22,30-33H,6-7H2,1H3,(H3-,23,24,25,34,35,36,37)/t12-,13-,15-,16-,17-,18-,21-,22-/m1/s1
InChIKey
KPVQNXLUPNWQHM-RBEMOOQDSA-N
SMILES
Software
SMILES
OpenEye OEToolkits 1.7.5
CC(=O)c1ccc[n+](c1)C2C(C(C(O2)COP(=O)([O-])OP(=O)(O)OCC3C(C(C(O3)n4cnc5c4ncnc5N)O)O)O)O
CACTVS 3.385
CC(=O)c1ccc[n+](c1)[C@@H]2O[C@H](CO[P]([O-])(=O)O[P](O)(=O)OC[C@H]3O[C@H]([C@H](O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.7.5
CC(=O)c1ccc[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)COP(=O)([O-])O[P@](=O)(O)OC[C@@H]3[C@H]([C@H]([C@@H](O3)n4cnc5c4ncnc5N)O)O)O)O
CACTVS 3.385
CC(=O)c1ccc[n+](c1)[CH]2O[CH](CO[P]([O-])(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
Formula
C22 H28 N6 O14 P2
Name
3-ACETYLPYRIDINE ADENINE DINUCLEOTIDE
ChEMBL
DrugBank
DB03363
ZINC
PDB chain
1drv Chain A Residue 301 [
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Receptor-Ligand Complex Structure
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PDB
1drv
Interaction of pyridine nucleotide substrates with Escherichia coli dihydrodipicolinate reductase: thermodynamic and structural analysis of binary complexes.
Resolution
2.2 Å
Binding residue
(original residue number in PDB)
G12 G15 R16 M17 E38 F79 T80 R81 G84 G102 A127 F129 R240
Binding residue
(residue number reindexed from 1)
G9 G12 R13 M14 E35 F76 T77 R78 G81 G99 A124 F126 R237
Annotation score
4
Binding affinity
MOAD
: Kd=0.29uM
PDBbind-CN
: -logKd/Ki=6.54,Kd=0.29uM
Enzymatic activity
Catalytic site (original residue number in PDB)
H159 K163
Catalytic site (residue number reindexed from 1)
H156 K160
Enzyme Commision number
1.17.1.8
: 4-hydroxy-tetrahydrodipicolinate reductase.
Gene Ontology
Molecular Function
GO:0008839
4-hydroxy-tetrahydrodipicolinate reductase
GO:0016491
oxidoreductase activity
GO:0016726
oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor
GO:0042802
identical protein binding
GO:0050661
NADP binding
GO:0051287
NAD binding
Biological Process
GO:0008652
amino acid biosynthetic process
GO:0009085
lysine biosynthetic process
GO:0009089
lysine biosynthetic process via diaminopimelate
GO:0019877
diaminopimelate biosynthetic process
Cellular Component
GO:0005737
cytoplasm
GO:0005829
cytosol
View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1drv
,
PDBe:1drv
,
PDBj:1drv
PDBsum
1drv
PubMed
8873595
UniProt
P04036
|DAPB_ECOLI 4-hydroxy-tetrahydrodipicolinate reductase (Gene Name=dapB)
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