5MLD

Crystal Structure of RosB with bound intermediate AFP (8-demethyl-8-aminoriboflavin-5'-phosphate)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008483	molecular_function	transaminase activity
A	0016491	molecular_function	oxidoreductase activity
A	0016740	molecular_function	transferase activity
A	0016999	biological_process	antibiotic metabolic process
A	0017000	biological_process	antibiotic biosynthetic process
B	0008483	molecular_function	transaminase activity
B	0016491	molecular_function	oxidoreductase activity
B	0016740	molecular_function	transferase activity
B	0016999	biological_process	antibiotic metabolic process
B	0017000	biological_process	antibiotic biosynthetic process
C	0008483	molecular_function	transaminase activity
C	0016491	molecular_function	oxidoreductase activity
C	0016740	molecular_function	transferase activity
C	0016999	biological_process	antibiotic metabolic process
C	0017000	biological_process	antibiotic biosynthetic process
D	0008483	molecular_function	transaminase activity
D	0016491	molecular_function	oxidoreductase activity
D	0016740	molecular_function	transferase activity
D	0016999	biological_process	antibiotic metabolic process
D	0017000	biological_process	antibiotic biosynthetic process
E	0008483	molecular_function	transaminase activity
E	0016491	molecular_function	oxidoreductase activity
E	0016740	molecular_function	transferase activity
E	0016999	biological_process	antibiotic metabolic process
E	0017000	biological_process	antibiotic biosynthetic process
F	0008483	molecular_function	transaminase activity
F	0016491	molecular_function	oxidoreductase activity
F	0016740	molecular_function	transferase activity
F	0016999	biological_process	antibiotic metabolic process
F	0017000	biological_process	antibiotic biosynthetic process
G	0008483	molecular_function	transaminase activity
G	0016491	molecular_function	oxidoreductase activity
G	0016740	molecular_function	transferase activity
G	0016999	biological_process	antibiotic metabolic process
G	0017000	biological_process	antibiotic biosynthetic process
H	0008483	molecular_function	transaminase activity
H	0016491	molecular_function	oxidoreductase activity
H	0016740	molecular_function	transferase activity
H	0016999	biological_process	antibiotic metabolic process
H	0017000	biological_process	antibiotic biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	binding site for residue 8DP A 301

Chain	Residue
A	THR11
A	ASN94
A	CYS132
A	GLY133
A	ASN134
A	GLU135
A	ASP136
A	HOH409
A	HOH419
A	HOH454
B	TYR240
A	ARG13
B	HOH549
D	GLU105
A	SER19
A	GLN20
A	THR21
A	PRO90
A	ILE91
A	THR92
A	LEU93

---

site_id	AC2
Number of Residues	20
Details	binding site for residue 8DP B 301

Chain	Residue
A	TYR240
B	THR11
B	ARG13
B	SER19
B	GLN20
B	THR21
B	PRO90
B	ILE91
B	THR92
B	LEU93
B	ASN94
B	CYS132
B	GLY133
B	ASN134
B	GLU135
B	ASP136
B	HOH440
B	HOH449
B	HOH548
C	GLU105

---

site_id	AC3
Number of Residues	21
Details	binding site for residue 8DP C 301

Chain	Residue
B	GLU105
B	HOH569
C	THR11
C	ARG13
C	SER19
C	GLN20
C	THR21
C	PRO90
C	ILE91
C	THR92
C	LEU93
C	ASN94
C	CYS132
C	GLY133
C	ASN134
C	GLU135
C	ASP136
C	HOH412
C	HOH420
C	HOH465
D	TYR240

---

site_id	AC4
Number of Residues	23
Details	binding site for residue 8DP D 301

Chain	Residue
A	GLU105
C	TYR240
C	HOH484
D	THR11
D	ARG13
D	SER19
D	GLN20
D	THR21
D	PRO90
D	ILE91
D	THR92
D	LEU93
D	ASN94
D	CYS132
D	GLY133
D	ASN134
D	GLU135
D	ASP136
D	HOH408
D	HOH430
D	HOH491
D	HOH579
D	HOH582

---

site_id	AC5
Number of Residues	23
Details	binding site for residue 8DP E 301

Chain	Residue
E	ASP136
E	HOH405
E	HOH441
E	HOH491
E	HOH520
E	HOH533
E	HOH550
G	TYR240
H	GLU105
E	THR11
E	ARG13
E	SER19
E	GLN20
E	THR21
E	PRO90
E	ILE91
E	THR92
E	LEU93
E	ASN94
E	CYS132
E	GLY133
E	ASN134
E	GLU135

---

site_id	AC6
Number of Residues	20
Details	binding site for residue 8DP F 301

Chain	Residue
F	THR11
F	ARG13
F	SER19
F	GLN20
F	THR21
F	PRO90
F	ILE91
F	THR92
F	LEU93
F	ASN94
F	CYS132
F	GLY133
F	ASN134
F	GLU135
F	ASP136
F	HOH446
F	HOH496
F	HOH545
G	GLU105
H	TYR240

---

site_id	AC7
Number of Residues	22
Details	binding site for residue 8DP G 301

Chain	Residue
E	TYR240
F	GLU105
G	THR11
G	ARG13
G	SER19
G	GLN20
G	THR21
G	PRO90
G	ILE91
G	THR92
G	LEU93
G	ASN94
G	CYS132
G	GLY133
G	ASN134
G	GLU135
G	ASP136
G	HOH411
G	HOH416
G	HOH448
G	HOH555
G	HOH575

---

site_id	AC8
Number of Residues	20
Details	binding site for residue 8DP H 301

Chain	Residue
E	GLU105
F	TYR240
H	THR11
H	ARG13
H	SER19
H	GLN20
H	THR21
H	PRO90
H	ILE91
H	THR92
H	LEU93
H	ASN94
H	CYS132
H	GLY133
H	ASN134
H	GLU135
H	ASP136
H	HOH436
H	HOH454
H	HOH534

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	88
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27981706","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5MJI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MLD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27981706","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	Site: {"description":"Important to position the amino-group donor glutamate","evidences":[{"source":"PubMed","id":"27981706","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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