3SRV

Crystal structure of spleen tyrosine kinase (SYK) in complex with a diaminopyrimidine carboxamide inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004713	molecular_function	protein tyrosine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
B	0004672	molecular_function	protein kinase activity
B	0004713	molecular_function	protein tyrosine kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE S19 A 1

Chain	Residue
A	GOL2
A	ARG498
A	ASN499
A	LEU501
A	SER511
A	ASP512
A	HOH52
A	HOH235
A	ALA400
A	MET448
A	GLU449
A	ALA451
A	GLY454
A	PRO455

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 636

Chain	Residue
A	HOH76
A	HOH202
A	MET424
A	LEU427
A	ARG434
A	MET435
A	HOH637

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 2

Chain	Residue
A	S191
A	LYS402
A	ASP494
A	ARG498
A	ASN499
A	ASP512

---

site_id	AC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GOL A 3

Chain	Residue
A	LYS458

---

site_id	AC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE S19 B 2

Chain	Residue
B	HOH52
B	HOH199
B	LEU377
B	SER379
B	ALA400
B	VAL433
B	MET448
B	GLU449
B	MET450
B	ALA451
B	GLY454
B	PRO455
B	ARG498
B	ASN499
B	LEU501
B	SER511
B	ASP512

---

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 4

Chain	Residue
B	HOH32
B	GLN461
B	LYS571

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	26
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGNFGTVKkGyyqmkkvvkt........VAVK

Chain	Residue	Details
B	LEU377-LYS402
A	LEU377-LYS402

---

site_id	PS00109
Number of Residues	13
Details	PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNVLL

Chain	Residue	Details
B	PHE490-LEU502
A	PHE490-LEU502

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	11
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"21469132","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"21469132","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"21469132","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P48025","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21469132","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18369315","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21469132","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---