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PDBsum entry 3w8q

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protein ligands links
Transferase PDB id
3w8q

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
318 a.a.
Ligands
AGS
Waters ×57
PDB id:
3w8q
Name: Transferase
Title: Structure of the human mitogen-activated protein kinase kinase 1 (mek1)
Structure: Dual specificity mitogen-activated protein kinase kinase 1. Chain: a. Fragment: kinase domain, unp residues 39-382. Synonym: map kinase kinase 1, mapkk 1, mkk1, erk activator kinase 1, mapk/erk kinase 1, mek 1. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: map2k1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.20Å     R-factor:   0.201     R-free:   0.268
Authors: S.Nakae,M.Kitamura,T.Shirai,T.Tada
Key ref: S.Nakae et al. Structure of the human mitogen-Activated protein kina kinase 1 (mek1) in "dfg-Asp out" conformation. To be published, . PubMed id: 34866601
Date:
20-Mar-13     Release date:   26-Mar-14    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q02750  (MP2K1_HUMAN) -  Dual specificity mitogen-activated protein kinase kinase 1 from Homo sapiens
Seq:
Struc:
393 a.a.
318 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.7.12.2  - mitogen-activated protein kinase kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction:
1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H+
3. L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H+
L-seryl-[protein]
Bound ligand (Het Group name = AGS)
matches with 93.75% similarity
+ ATP
= O-phospho-L-seryl-[protein]
+ ADP
+ H(+)
L-threonyl-[protein]
Bound ligand (Het Group name = AGS)
matches with 93.75% similarity
+ ATP
= O-phospho-L-threonyl-[protein]
+ ADP
+ H(+)
L-tyrosyl-[protein]
Bound ligand (Het Group name = AGS)
matches with 93.75% similarity
+ ATP
= O-phospho-L-tyrosyl-[protein]
+ ADP
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 

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