6CBL

x-ray structure of NeoB from Streptomyces fradiae in complex with neamine as an external aldimine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008483	molecular_function	transaminase activity
A	0016740	molecular_function	transferase activity
A	0017000	biological_process	antibiotic biosynthetic process
A	0030170	molecular_function	pyridoxal phosphate binding
A	1901158	biological_process	neomycin biosynthetic process
B	0008483	molecular_function	transaminase activity
B	0016740	molecular_function	transferase activity
B	0017000	biological_process	antibiotic biosynthetic process
B	0030170	molecular_function	pyridoxal phosphate binding
B	1901158	biological_process	neomycin biosynthetic process
C	0008483	molecular_function	transaminase activity
C	0016740	molecular_function	transferase activity
C	0017000	biological_process	antibiotic biosynthetic process
C	0030170	molecular_function	pyridoxal phosphate binding
C	1901158	biological_process	neomycin biosynthetic process
D	0008483	molecular_function	transaminase activity
D	0016740	molecular_function	transferase activity
D	0017000	biological_process	antibiotic biosynthetic process
D	0030170	molecular_function	pyridoxal phosphate binding
D	1901158	biological_process	neomycin biosynthetic process
E	0008483	molecular_function	transaminase activity
E	0016740	molecular_function	transferase activity
E	0017000	biological_process	antibiotic biosynthetic process
E	0030170	molecular_function	pyridoxal phosphate binding
E	1901158	biological_process	neomycin biosynthetic process
F	0008483	molecular_function	transaminase activity
F	0016740	molecular_function	transferase activity
F	0017000	biological_process	antibiotic biosynthetic process
F	0030170	molecular_function	pyridoxal phosphate binding
F	1901158	biological_process	neomycin biosynthetic process
G	0008483	molecular_function	transaminase activity
G	0016740	molecular_function	transferase activity
G	0017000	biological_process	antibiotic biosynthetic process
G	0030170	molecular_function	pyridoxal phosphate binding
G	1901158	biological_process	neomycin biosynthetic process
H	0008483	molecular_function	transaminase activity
H	0016740	molecular_function	transferase activity
H	0017000	biological_process	antibiotic biosynthetic process
H	0030170	molecular_function	pyridoxal phosphate binding
H	1901158	biological_process	neomycin biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	25
Details	binding site for residue DOW A 501

Chain	Residue
A	THR13
A	VAL206
A	LYS207
A	LYS231
A	TYR341
A	ASP344
A	ASN391
A	VAL392
A	ASP394
A	HOH611
A	HOH651
A	ARG48
A	HOH702
A	HOH722
A	HOH730
A	HOH810
B	PHE257
B	THR258
A	GLY104
A	THR105
A	TYR129
A	HIS130
A	GLY131
A	SER176
A	ASP204

---

site_id	AC2
Number of Residues	5
Details	binding site for residue CL A 502

Chain	Residue
A	PHE155
A	LEU157
A	TRP186
A	HOH854
A	HOH929

---

site_id	AC3
Number of Residues	26
Details	binding site for residue DOW B 501

Chain	Residue
A	PHE257
A	THR258
A	HOH699
B	THR13
B	ARG48
B	SER103
B	GLY104
B	THR105
B	TYR129
B	HIS130
B	GLY131
B	SER176
B	ASP204
B	VAL206
B	LYS207
B	LYS231
B	TYR341
B	ASP344
B	ASN391
B	VAL392
B	ASP394
B	HOH643
B	HOH672
B	HOH676
B	HOH717
B	HOH719

---

site_id	AC4
Number of Residues	26
Details	binding site for residue DOW C 501

Chain	Residue
C	THR13
C	ARG48
C	GLY104
C	THR105
C	TYR129
C	HIS130
C	GLY131
C	SER176
C	ASP204
C	VAL206
C	LYS207
C	LYS231
C	TYR341
C	ASP344
C	ASN391
C	VAL392
C	ASP394
C	HOH646
C	HOH693
C	HOH696
C	HOH706
C	HOH733
C	HOH781
C	HOH816
D	PHE257
D	THR258

---

site_id	AC5
Number of Residues	25
Details	binding site for residue DOW D 501

Chain	Residue
D	ASN391
D	VAL392
D	ASP394
D	HOH2534
D	HOH2571
D	HOH2584
D	HOH2591
D	HOH2623
C	PHE257
C	THR258
C	HOH701
D	ARG48
D	SER103
D	GLY104
D	THR105
D	TYR129
D	HIS130
D	GLY131
D	SER176
D	ASP204
D	VAL206
D	LYS207
D	LYS231
D	TYR341
D	ASP344

---

site_id	AC6
Number of Residues	25
Details	binding site for residue DOW E 501

Chain	Residue
E	THR13
E	ARG48
E	GLY104
E	THR105
E	TYR129
E	HIS130
E	GLY131
E	SER176
E	ASP204
E	VAL206
E	LYS207
E	LYS231
E	TYR341
E	ASP344
E	ASN391
E	VAL392
E	ASP394
E	HOH642
E	HOH643
E	HOH661
E	HOH703
E	HOH709
E	HOH761
F	PHE257
F	THR258

---

site_id	AC7
Number of Residues	23
Details	binding site for residue DOW F 501

Chain	Residue
E	PHE257
E	THR258
F	ARG48
F	GLY104
F	THR105
F	TYR129
F	HIS130
F	GLY131
F	SER176
F	ASP204
F	VAL206
F	LYS207
F	LYS231
F	TYR341
F	ASP344
F	ASN391
F	VAL392
F	ASP394
F	HOH624
F	HOH635
F	HOH684
F	HOH689
F	HOH728

---

site_id	AC8
Number of Residues	26
Details	binding site for residue DOW G 501

Chain	Residue
G	ARG48
G	SER103
G	GLY104
G	THR105
G	TYR129
G	HIS130
G	GLY131
G	SER176
G	ASP204
G	VAL206
G	LYS207
G	LYS231
G	TYR341
G	ASP344
G	ASN391
G	VAL392
G	ASP394
G	HOH619
G	HOH624
G	HOH635
G	HOH666
G	HOH681
G	HOH725
H	PHE257
H	THR258
H	HOH623

---

site_id	AC9
Number of Residues	24
Details	binding site for residue DOW H 501

Chain	Residue
G	PHE257
G	THR258
H	THR13
H	ARG48
H	GLY104
H	THR105
H	TYR129
H	HIS130
H	GLY131
H	SER176
H	ASP204
H	VAL206
H	LYS207
H	LYS231
H	TYR341
H	ASP344
H	ASN391
H	VAL392
H	ASP394
H	HOH614
H	HOH638
H	HOH665
H	HOH715
H	HOH746

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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