4XG8

Crystal structure of an inhibitor-bound Syk

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
C	0004672	molecular_function	protein kinase activity
C	0004713	molecular_function	protein tyrosine kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue X8G A 700

Chain	Residue
A	LEU377
A	LEU501
A	ASP512
A	MET448
A	GLU449
A	MET450
A	ALA451
A	GLY454
A	PRO455
A	ARG498
A	ASN499

---

site_id	AC2
Number of Residues	15
Details	binding site for residue X8G C 700

Chain	Residue
C	LEU377
C	GLY378
C	VAL385
C	ALA400
C	MET448
C	GLU449
C	MET450
C	ALA451
C	GLY454
C	PRO455
C	ARG498
C	ASN499
C	LEU501
C	SER511
C	ASP512

---

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
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
A	PHE490-LEU502

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028

Chain	Residue	Details
A	ASP494
C	ASP494

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU377
A	LYS402
C	LEU377
C	LYS402

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:21469132

Chain	Residue	Details
A	TYR364
C	TYR526
C	TYR629
C	TYR631
A	TYR484
A	TYR507
A	TYR526
A	TYR629
A	TYR631
C	TYR364
C	TYR484
C	TYR507

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:21469132

Chain	Residue	Details
A	SER379
A	SER579
C	SER379
C	SER579

---

site_id	SWS_FT_FI5
Number of Residues	6
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:21469132

Chain	Residue	Details
A	THR384
A	THR530
A	THR582
C	THR384
C	THR530
C	THR582

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:21469132

Chain	Residue	Details
A	TYR525
C	TYR525

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P48025

Chain	Residue	Details
A	TYR546
C	TYR546

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:18369315, ECO:0000269|PubMed:21469132

Chain	Residue	Details
A	TYR630
C	TYR630

---