Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7MMS

Crystal Structure of the Class Ie Ribonucleotide Reductase Beta-NrdI complex from Aerococcus urinae in Semiquinone Form with Cu(I) bound

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004748	molecular_function	ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
A	0005971	cellular_component	ribonucleoside-diphosphate reductase complex
A	0009263	biological_process	deoxyribonucleotide biosynthetic process
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0046872	molecular_function	metal ion binding
B	0004748	molecular_function	ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
B	0005971	cellular_component	ribonucleoside-diphosphate reductase complex
B	0009263	biological_process	deoxyribonucleotide biosynthetic process
B	0016020	cellular_component	membrane
B	0016491	molecular_function	oxidoreductase activity
B	0046872	molecular_function	metal ion binding
C	0004748	molecular_function	ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
C	0005971	cellular_component	ribonucleoside-diphosphate reductase complex
C	0009263	biological_process	deoxyribonucleotide biosynthetic process
C	0016020	cellular_component	membrane
C	0016491	molecular_function	oxidoreductase activity
C	0046872	molecular_function	metal ion binding
D	0004748	molecular_function	ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
D	0005971	cellular_component	ribonucleoside-diphosphate reductase complex
D	0009263	biological_process	deoxyribonucleotide biosynthetic process
D	0016020	cellular_component	membrane
D	0016491	molecular_function	oxidoreductase activity
D	0046872	molecular_function	metal ion binding
E	0000166	molecular_function	nucleotide binding
E	0010181	molecular_function	FMN binding
E	0036211	biological_process	protein modification process
F	0000166	molecular_function	nucleotide binding
F	0010181	molecular_function	FMN binding
F	0036211	biological_process	protein modification process
G	0000166	molecular_function	nucleotide binding
G	0010181	molecular_function	FMN binding
G	0036211	biological_process	protein modification process
H	0000166	molecular_function	nucleotide binding
H	0010181	molecular_function	FMN binding
H	0036211	biological_process	protein modification process

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue CU1 A 401

Chain	Residue
A	VAL116
A	PRO176
A	HIS213
A	HOH545
A	HOH590

site_id	AC2
Number of Residues	8
Details	binding site for residue GOL A 402

Chain	Residue
A	PHE262
A	GLY263
A	LEU264
A	ALA265
A	HIS256
A	TYR259
A	ASP260
A	GLY261

site_id	AC3
Number of Residues	10
Details	binding site for residue GOL A 403

Chain	Residue
A	TYR6
A	SER11
A	ARG25
A	SER100
A	LEU101
A	THR102
A	GLU103
A	GLN106
A	HOH561
A	HOH605

site_id	AC4
Number of Residues	4
Details	binding site for residue CA A 404

Chain	Residue
A	GLU52
A	ARG121
B	TRP41
B	HOH558

site_id	AC5
Number of Residues	5
Details	binding site for residue CU1 B 401

Chain	Residue
B	VAL116
B	PRO176
B	HIS213
B	HOH555
B	HOH578

site_id	AC6
Number of Residues	3
Details	binding site for residue GOL B 402

Chain	Residue
B	GLU333
B	TRP335
B	PHE337

site_id	AC7
Number of Residues	6
Details	binding site for residue GOL B 403

Chain	Residue
B	TYR6
B	SER11
B	ARG25
B	SER100
B	LEU101
B	GLN106

site_id	AC8
Number of Residues	4
Details	binding site for residue CA B 404

Chain	Residue
A	TRP41
A	HOH560
B	GLU52
B	ARG121

site_id	AC9
Number of Residues	5
Details	binding site for residue CU1 C 401

Chain	Residue
C	VAL116
C	PRO176
C	HIS213
C	HOH527
C	HOH598

site_id	AD1
Number of Residues	7
Details	binding site for residue GOL C 402

Chain	Residue
C	TYR6
C	SER11
C	ARG25
C	SER100
C	LEU101
C	GLN106
C	HOH502

site_id	AD2
Number of Residues	1
Details	binding site for residue CU1 C 403

Chain	Residue
C	HIS256

site_id	AD3
Number of Residues	3
Details	binding site for residue CA C 404

Chain	Residue
C	GLY263
C	ASP266
C	GLU267

site_id	AD4
Number of Residues	6
Details	binding site for residue GOL D 401

Chain	Residue
D	TYR6
D	ARG25
D	SER100
D	LEU101
D	GLN106
D	HOH544

site_id	AD5
Number of Residues	22
Details	binding site for residue FNR E 201

Chain	Residue
A	PHE215
E	SER9
E	THR10
E	SER12
E	ASN13
E	ASN14
E	THR15
E	PRO48
E	THR49
E	TYR50
E	SER51
E	GLY52
E	GLY53
E	GLY91
E	ASN92
E	PHE95
E	SER98
E	PHE99
E	ALA100
E	LEU120
E	HOH309
E	HOH320

site_id	AD6
Number of Residues	3
Details	binding site for residue GOL E 202

Chain	Residue
A	GLU39
E	TYR50
E	GLN70

site_id	AD7
Number of Residues	22
Details	binding site for residue FNR G 201

Chain	Residue
G	THR49
G	TYR50
G	SER51
G	GLY52
G	GLY53
G	GLY91
G	ASN92
G	PHE95
G	SER98
G	PHE99
G	ALA100
G	LEU120
G	HOH308
G	HOH313
G	HOH315
G	SER9
G	THR10
G	SER12
G	ASN13
G	ASN14
G	THR15
G	PRO48

site_id	AD8
Number of Residues	8
Details	binding site for residue GOL F 501

Chain	Residue
B	ARG204
B	ALA302
B	GLN303
B	LEU304
B	SER305
B	ALA306
F	GLY96
F	ASP97

site_id	AD9
Number of Residues	25
Details	binding site for residue FNR F 502

Chain	Residue
B	GLU39
B	ARG43
B	PHE215
F	SER9
F	THR10
F	SER12
F	ASN13
F	ASN14
F	THR15
F	PRO48
F	THR49
F	TYR50
F	SER51
F	GLY52
F	GLY53
F	GLY91
F	ASN92
F	PHE95
F	SER98
F	PHE99
F	ALA100
F	LEU120
F	HOH614
F	HOH627
F	HOH628

site_id	AE1
Number of Residues	5
Details	binding site for residue GOL F 503

Chain	Residue
B	GLU39
F	TYR50
F	PRO68
F	GLN70
F	HOH622

site_id	AE2
Number of Residues	21
Details	binding site for residue FNR H 201

Chain	Residue
D	GLU39
H	SER9
H	THR10
H	SER12
H	ASN13
H	ASN14
H	THR15
H	PRO48
H	THR49
H	TYR50
H	SER51
H	GLY52
H	GLY91
H	ASN92
H	PHE95
H	SER98
H	PHE99
H	ALA100
H	LEU120
H	HOH305
H	HOH311

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)