Structure of PDB 1zak Chain B

Receptor sequence
>1zakB (length=220) Species: 4577 (Zea mays) [Search protein sequence]
ADPLKVMISGAPASGKGTQCELIKTKYQLAHISAGDLLRAEIAAGSENGK
RAKEFMEKGQLVPDEIVVNMVKERLRQPDAQENGWLLDGYPRSYSQAMAL
ETLEIRPDTFILLDVPDELLVERVVGRRLDPVTGKIYHLKYSPPENEEIA
SRLTQRFDDTEEKVKLRLETYYQNIESLLSTYENIIVKVQGDATVDAVFA
KIDELLGSILEKKNEMVSST
3D structure
PDB1zak Structure, catalysis and supramolecular assembly of adenylate kinase from maize.
ChainB
Resolution3.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K18 R94 R129 R158 R169
Catalytic site (residue number reindexed from 1) K16 R92 R127 R156 R167
Enzyme Commision number 2.7.4.3: adenylate kinase.
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 AP5 B P14 A15 S16 G17 K18 G19 T20 L40 R41 M58 Q62 V64 G91 R94 Q98 R125 R129 I138 H140 Y143 R158 A195 V197 P12 A13 S14 G15 K16 G17 T18 L38 R39 M56 Q60 V62 G89 R92 Q96 R123 R127 I136 H138 Y141 R156 A193 V195
Gene Ontology
Molecular Function
GO:0004017 adenylate kinase activity
GO:0004127 (d)CMP kinase activity
GO:0004550 nucleoside diphosphate kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0016776 phosphotransferase activity, phosphate group as acceptor
GO:0019205 nucleobase-containing compound kinase activity
Biological Process
GO:0006139 nucleobase-containing compound metabolic process
GO:0016310 phosphorylation
GO:0046940 nucleoside monophosphate phosphorylation
Cellular Component
GO:0005737 cytoplasm
GO:0009507 chloroplast

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1zak, PDBe:1zak, PDBj:1zak
PDBsum1zak
PubMed9428681
UniProtP43188|KADC_MAIZE Adenylate kinase, chloroplastic (Gene Name=ADK1)

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