Structure of PDB 6yg2 Chain A

Receptor sequence
>6yg2A (length=290) Species: 9606 (Homo sapiens) [Search protein sequence]
QTGYLTIGGQRYQAEINDLENLGEMGSGTCGQVWKMRFRKTGHVIAVKQM
RRSGNKEENKRILMDLDVVLKSHDCPYIVQCFGTFITNTDVFIAMELMGT
CAEKLKKRMQGPIPERILGKMTVAIVKALYYLKEKHGVIHRDVKPSNILL
DERGQIKLCDFGISGCAAYMAPERIDPPDPTKPDYDIRADVWSLGISLVE
LATGQFPYKNCKTDFEVLTKVLQEEPPLLPGHMGFSGDFQSFVKDCLTKD
HRKRPKYNKLLEHSFIKRYETLEVDVASWFKDVMAKTESP
3D structure
PDB6yg2 Catalytic Domain Plasticity of MKK7 Reveals Structural Mechanisms of Allosteric Activation and Diverse Targeting Opportunities.
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) D259 K261 N264 D277 C296
Catalytic site (residue number reindexed from 1) D142 K144 N147 D160 C166
Enzyme Commision number 2.7.12.2: mitogen-activated protein kinase 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 1E8 A Y121 L122 I133 L136 W151 M153 G200 T201 F202 F209 A211 Y4 L5 I16 L19 W34 M36 G83 T84 F85 F92 A94
BS02 8E8 A M142 G145 K165 I179 L183 M212 E213 L214 M215 C218 K221 M25 G28 K48 I62 L66 M95 E96 L97 M98 C101 K104
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:6yg2, PDBe:6yg2, PDBj:6yg2
PDBsum6yg2
PubMed32783966
UniProtO14733|MP2K7_HUMAN Dual specificity mitogen-activated protein kinase kinase 7 (Gene Name=MAP2K7)

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