1OZ0

CRYSTAL STRUCTURE OF THE HOMODIMERIC BIFUNCTIONAL TRANSFORMYLASE AND CYCLOHYDROLASE ENZYME AVIAN ATIC IN COMPLEX WITH A MULTISUBSTRATE ADDUCT INHIBITOR BETA-DADF.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0003937	molecular_function	IMP cyclohydrolase activity
A	0004643	molecular_function	phosphoribosylaminoimidazolecarboxamide formyltransferase activity
A	0005829	cellular_component	cytosol
A	0006164	biological_process	purine nucleotide biosynthetic process
A	0006189	biological_process	'de novo' IMP biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016787	molecular_function	hydrolase activity
A	0042803	molecular_function	protein homodimerization activity
B	0003824	molecular_function	catalytic activity
B	0003937	molecular_function	IMP cyclohydrolase activity
B	0004643	molecular_function	phosphoribosylaminoimidazolecarboxamide formyltransferase activity
B	0005829	cellular_component	cytosol
B	0006164	biological_process	purine nucleotide biosynthetic process
B	0006189	biological_process	'de novo' IMP biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016787	molecular_function	hydrolase activity
B	0042803	molecular_function	protein homodimerization activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K B 1003

Chain	Residue
B	VAL426
B	THR429
B	SER431
B	SER433
B	ASP540
B	LEU590
B	HIS592

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K A 1004

Chain	Residue
A	SER431
A	SER433
A	ASP540
A	LEU590
A	HIS592
A	VAL426
A	THR429

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 A 1005

Chain	Residue
A	SER11
A	SER35
A	GLY36
A	GLY37
A	THR38

---

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 B 1006

Chain	Residue
B	SER11
B	LYS15
B	SER35
B	GLY36
B	GLY37
B	THR38
B	LYS67

---

site_id	AC5
Number of Residues	34
Details	BINDING SITE FOR RESIDUE MS1 B 1001

Chain	Residue
A	ARG208
A	TYR209
A	ILE239
A	ASN240
A	LYS267
A	MET313
A	PHE316
A	GLY317
A	ASP340
A	HOH1034
A	HOH1063
B	GLN450
B	SER451
B	ARG452
B	ILE453
B	ALA541
B	PHE542
B	PRO544
B	PHE545
B	ASP547
B	SER566
B	ALA567
B	ARG589
B	PHE591
B	HOH1007
B	HOH1008
B	HOH1028
B	HOH1037
B	HOH1047
B	HOH1092
B	HOH1117
B	HOH1127
B	HOH1160
B	HOH1180

---

site_id	AC6
Number of Residues	28
Details	BINDING SITE FOR RESIDUE MS1 A 1002

Chain	Residue
A	GLN450
A	ARG452
A	ILE453
A	ALA541
A	PHE542
A	PHE545
A	ASP547
A	SER566
A	ALA567
A	ARG589
A	PHE591
A	HOH1021
A	HOH1034
A	HOH1042
A	HOH1065
A	HOH1130
A	HOH1144
A	HOH1145
A	HOH1168
A	HOH1203
B	ARG208
B	TYR209
B	ILE239
B	LYS267
B	MET313
B	PHE316
B	GLY317
B	ASP340

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	786
Details	Region: {"description":"AICAR formyltransferase","evidences":[{"source":"PubMed","id":"17324932","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton donor/acceptor; for FAICAR cyclization activity","evidences":[{"source":"UniProtKB","id":"P31939","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Active site: {"description":"Proton acceptor; for AICAR formyltransferase activity","evidences":[{"source":"UniProtKB","id":"P31939","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11323713","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"12501179","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1G8M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1M9N","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12501179","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1M9N","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	8
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"12501179","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1M9N","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P31939","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12974624","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1OZ0","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12501179","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1M9N","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P31939","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P31939","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1p4r

Chain	Residue	Details
A	HIS593
A	ASN432
A	HIS268
A	LYS267

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1p4r

Chain	Residue	Details
B	HIS593
B	ASN432
B	HIS268
B	LYS267

---