2IPI

Crystal Structure of Aclacinomycin Oxidoreductase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0016491	molecular_function	oxidoreductase activity
A	0017000	biological_process	antibiotic biosynthetic process
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0071949	molecular_function	FAD binding
B	0000166	molecular_function	nucleotide binding
B	0016491	molecular_function	oxidoreductase activity
B	0017000	biological_process	antibiotic biosynthetic process
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0071949	molecular_function	FAD binding
C	0000166	molecular_function	nucleotide binding
C	0016491	molecular_function	oxidoreductase activity
C	0017000	biological_process	antibiotic biosynthetic process
C	0050660	molecular_function	flavin adenine dinucleotide binding
C	0071949	molecular_function	FAD binding
D	0000166	molecular_function	nucleotide binding
D	0016491	molecular_function	oxidoreductase activity
D	0017000	biological_process	antibiotic biosynthetic process
D	0050660	molecular_function	flavin adenine dinucleotide binding
D	0071949	molecular_function	FAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE AKY A 601

Chain	Residue
A	PHE72
A	TRP409
A	TYR450
A	FAD801
A	HOH936
A	HOH1060
A	HOH1071
A	ASP335
A	THR336
A	PHE339
A	TRP372
A	TYR378
A	TRP404
A	SER406
A	THR408

---

site_id	AC2
Number of Residues	29
Details	BINDING SITE FOR RESIDUE FAD A 801

Chain	Residue
A	PHE29
A	VAL65
A	ARG66
A	SER67
A	GLY68
A	GLY69
A	HIS70
A	CYS71
A	VAL76
A	GLY128
A	VAL129
A	CYS130
A	VAL133
A	GLY134
A	GLY137
A	HIS138
A	GLY143
A	TYR144
A	GLY197
A	GLY198
A	GLY201
A	VAL203
A	PHE447
A	ASN449
A	AKY601
A	HOH959
A	HOH964
A	HOH985
A	HOH989

---

site_id	AC3
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD B 801

Chain	Residue
B	PHE29
B	VAL65
B	ARG66
B	SER67
B	GLY68
B	GLY69
B	HIS70
B	CYS71
B	MET87
B	PRO106
B	GLY128
B	VAL129
B	CYS130
B	VAL133
B	GLY134
B	GLY137
B	HIS138
B	TYR144
B	GLY197
B	GLY201
B	ILE202
B	VAL203
B	PHE447
B	ASN449
B	HOH837
B	HOH939
B	HOH964
B	HOH971

---

site_id	AC4
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD C 801

Chain	Residue
C	HOH1109
C	PHE29
C	VAL65
C	ARG66
C	SER67
C	GLY68
C	GLY69
C	HIS70
C	CYS71
C	PHE72
C	VAL76
C	PRO106
C	GLY128
C	VAL129
C	CYS130
C	VAL133
C	GLY134
C	GLY137
C	HIS138
C	LEU140
C	TYR144
C	GLY197
C	GLY201
C	VAL203
C	PHE447
C	ASN449
C	HOH860
C	HOH873

---

site_id	AC5
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD D 801

Chain	Residue
D	PHE29
D	VAL65
D	ARG66
D	SER67
D	GLY68
D	GLY69
D	HIS70
D	CYS71
D	PHE72
D	PRO106
D	GLY128
D	VAL129
D	CYS130
D	VAL133
D	GLY134
D	GLY137
D	HIS138
D	GLY143
D	TYR144
D	GLY197
D	GLY198
D	GLY201
D	VAL203
D	PHE447
D	ASN449
D	HIS494
D	HOH918
D	HOH949

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	720
Details	Domain: {"description":"FAD-binding PCMH-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00718","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17395717","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17395717","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2IPI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17395717","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	Cross-link: {"description":"6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-Cys)","evidences":[{"source":"PubMed","id":"17395717","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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