6YG4

Crystal structure of MKK7 (MAP2K7) in complex with K00007

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue EDO A 501

Chain	Residue
A	ASN138
A	TRP151
A	MET153
A	GLN166
A	GLN227
A	HOH620

---

site_id	AC2
Number of Residues	4
Details	binding site for residue EDO A 502

Chain	Residue
A	LYS274
A	PRO193
A	GLN272
A	ILE273

---

site_id	AC3
Number of Residues	4
Details	binding site for residue EDO A 503

Chain	Residue
A	GLU232
A	MET363
A	GLY364
A	HOH613

---

site_id	AC4
Number of Residues	1
Details	binding site for residue EDO A 504

Chain	Residue
A	ARG318

---

site_id	AC5
Number of Residues	3
Details	binding site for residue EDO A 505

Chain	Residue
A	GLY367
A	ASP368
A	ARG398

---

site_id	AC6
Number of Residues	1
Details	binding site for residue EDO A 506

Chain	Residue
A	ARG398

---

site_id	AC7
Number of Residues	8
Details	binding site for residue SU9 A 507

Chain	Residue
A	MET142
A	ALA163
A	MET212
A	GLU213
A	MET215
A	GLY216
A	THR217
A	ASP277

---

Functional Information from PROSITE/UniProt

site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDVKpsNILL

Chain	Residue	Details
A	VAL255-LEU267

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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