Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5ZCT

The crystal structure of the poly-alpha-L-glutamate peptides synthetase RimK at 2.05 angstrom resolution.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003824	molecular_function	catalytic activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006412	biological_process	translation
A	0009432	biological_process	SOS response
A	0016874	molecular_function	ligase activity
A	0018169	molecular_function	ribosomal S6-glutamic acid ligase activity
A	0036211	biological_process	protein modification process
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding
B	0003824	molecular_function	catalytic activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006412	biological_process	translation
B	0009432	biological_process	SOS response
B	0016874	molecular_function	ligase activity
B	0018169	molecular_function	ribosomal S6-glutamic acid ligase activity
B	0036211	biological_process	protein modification process
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
C	0000166	molecular_function	nucleotide binding
C	0003824	molecular_function	catalytic activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006412	biological_process	translation
C	0009432	biological_process	SOS response
C	0016874	molecular_function	ligase activity
C	0018169	molecular_function	ribosomal S6-glutamic acid ligase activity
C	0036211	biological_process	protein modification process
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
D	0000166	molecular_function	nucleotide binding
D	0003824	molecular_function	catalytic activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0006412	biological_process	translation
D	0009432	biological_process	SOS response
D	0016874	molecular_function	ligase activity
D	0018169	molecular_function	ribosomal S6-glutamic acid ligase activity
D	0036211	biological_process	protein modification process
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
E	0000166	molecular_function	nucleotide binding
E	0003824	molecular_function	catalytic activity
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0006412	biological_process	translation
E	0009432	biological_process	SOS response
E	0016874	molecular_function	ligase activity
E	0018169	molecular_function	ribosomal S6-glutamic acid ligase activity
E	0036211	biological_process	protein modification process
E	0042802	molecular_function	identical protein binding
E	0046872	molecular_function	metal ion binding
F	0000166	molecular_function	nucleotide binding
F	0003824	molecular_function	catalytic activity
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0006412	biological_process	translation
F	0009432	biological_process	SOS response
F	0016874	molecular_function	ligase activity
F	0018169	molecular_function	ribosomal S6-glutamic acid ligase activity
F	0036211	biological_process	protein modification process
F	0042802	molecular_function	identical protein binding
F	0046872	molecular_function	metal ion binding
G	0000166	molecular_function	nucleotide binding
G	0003824	molecular_function	catalytic activity
G	0005524	molecular_function	ATP binding
G	0005737	cellular_component	cytoplasm
G	0006412	biological_process	translation
G	0009432	biological_process	SOS response
G	0016874	molecular_function	ligase activity
G	0018169	molecular_function	ribosomal S6-glutamic acid ligase activity
G	0036211	biological_process	protein modification process
G	0042802	molecular_function	identical protein binding
G	0046872	molecular_function	metal ion binding
H	0000166	molecular_function	nucleotide binding
H	0003824	molecular_function	catalytic activity
H	0005524	molecular_function	ATP binding
H	0005737	cellular_component	cytoplasm
H	0006412	biological_process	translation
H	0009432	biological_process	SOS response
H	0016874	molecular_function	ligase activity
H	0018169	molecular_function	ribosomal S6-glutamic acid ligase activity
H	0036211	biological_process	protein modification process
H	0042802	molecular_function	identical protein binding
H	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	27
Details	binding site for residue ANP A 401

Chain	Residue
A	LYS100
A	TYR179
A	ILE180
A	PHE210
A	ARG211
A	SER212
A	ASN213
A	MET259
A	GLU260
A	MG402
A	HOH508
A	VAL139
A	HOH520
A	HOH552
A	HOH569
A	HOH584
A	HOH586
A	HOH587
A	HOH640
A	HOH668
A	LYS141
A	GLY145
A	THR146
A	GLN147
A	GLY148
A	GLN177
A	GLU178

site_id	AC2
Number of Residues	4
Details	binding site for residue MG A 402

Chain	Residue
A	ANP401
A	HOH508
A	HOH520
A	HOH586

site_id	AC3
Number of Residues	7
Details	binding site for residue SO4 A 403

Chain	Residue
A	ARG284
A	ARG288
A	HOH533
A	HOH583
A	HOH599
G	ARG284
G	ARG288

site_id	AC4
Number of Residues	5
Details	binding site for residue SO4 A 404

Chain	Residue
A	ARG189
A	ARG203
A	ASN213
A	LEU214
A	HOH515

site_id	AC5
Number of Residues	3
Details	binding site for residue SO4 A 405

Chain	Residue
A	ARG96
A	ARG102
A	HOH526

site_id	AC6
Number of Residues	4
Details	binding site for residue MG B 402

Chain	Residue
B	ARG189
B	ASP248
B	GLU260
B	ANP401

site_id	AC7
Number of Residues	26
Details	binding site for residue ANP C 401

Chain	Residue
C	LYS100
C	LYS141
C	GLY145
C	THR146
C	GLN147
C	GLY148
C	GLN177
C	GLU178
C	TYR179
C	ILE180
C	PHE210
C	ARG211
C	SER212
C	ASN213
C	LEU250
C	MET259
C	GLU260
C	MG402
C	HOH513
C	HOH514
C	HOH551
C	HOH557
C	HOH564
C	HOH601
C	HOH606
C	HOH623

site_id	AC8
Number of Residues	4
Details	binding site for residue MG C 402

Chain	Residue
C	ANP401
C	HOH513
C	HOH514
C	HOH623

site_id	AC9
Number of Residues	6
Details	binding site for residue SO4 C 403

Chain	Residue
C	GLN147
C	ARG189
C	ARG203
C	ASN213
C	LEU214
C	HOH513

site_id	AD1
Number of Residues	5
Details	binding site for residue SO4 C 404

Chain	Residue
C	ARG96
C	ARG102
C	ARG109
C	HOH537
D	VAL92

site_id	AD2
Number of Residues	7
Details	binding site for residue SO4 C 405

Chain	Residue
C	ARG284
C	ARG288
C	HOH547
C	HOH552
C	HOH614
E	ARG284
E	ARG288

site_id	AD3
Number of Residues	20
Details	binding site for residue ANP D 401

Chain	Residue
D	VAL139
D	LYS141
D	VAL151
D	GLN177
D	GLU178
D	TYR179
D	ILE180
D	ASP187
D	ARG203
D	PHE210
D	ARG211
D	SER212
D	ASN213
D	MET259
D	GLU260
D	MG402
D	HOH506
D	HOH523
D	HOH556
D	LYS100

site_id	AD4
Number of Residues	5
Details	binding site for residue MG D 402

Chain	Residue
D	ASN213
D	GLU260
D	ANP401
D	HOH506
D	HOH523

site_id	AD5
Number of Residues	3
Details	binding site for residue SO4 D 403

Chain	Residue
C	VAL92
D	ARG102
D	HOH514

site_id	AD6
Number of Residues	4
Details	binding site for residue MG E 403

Chain	Residue
E	ANP402
E	HOH502
E	HOH559
E	HOH564

site_id	AD7
Number of Residues	5
Details	binding site for residue SO4 E 404

Chain	Residue
E	ARG96
E	ARG102
E	LEU106
E	HOH575
F	VAL92

site_id	AD8
Number of Residues	18
Details	binding site for residue ANP F 401

Chain	Residue
F	LYS100
F	LYS141
F	VAL151
F	GLN177
F	GLU178
F	TYR179
F	ILE180
F	PHE210
F	ARG211
F	SER212
F	ASN213
F	HIS215
F	ARG216
F	LEU250
F	MET259
F	GLU260
F	MG402
F	HOH510

site_id	AD9
Number of Residues	3
Details	binding site for residue MG F 402

Chain	Residue
F	ASN213
F	GLU260
F	ANP401

site_id	AE1
Number of Residues	4
Details	binding site for residue SO4 F 403

Chain	Residue
F	ARG96
F	ARG102
F	LEU106
F	HOH502

site_id	AE2
Number of Residues	27
Details	binding site for residue ANP G 401

Chain	Residue
G	LYS100
G	LYS141
G	GLY145
G	THR146
G	GLN147
G	GLY148
G	GLN177
G	GLU178
G	ILE180
G	ASP187
G	PHE210
G	ARG211
G	SER212
G	ASN213
G	LEU250
G	MET259
G	GLU260
G	MG402
G	HOH505
G	HOH516
G	HOH532
G	HOH569
G	HOH576
G	HOH581
G	HOH582
G	HOH583
G	HOH638

site_id	AE3
Number of Residues	4
Details	binding site for residue MG G 402

Chain	Residue
G	ANP401
G	HOH505
G	HOH532
G	HOH576

site_id	AE4
Number of Residues	4
Details	binding site for residue SO4 G 404

Chain	Residue
G	ARG96
G	ARG102
G	LEU106
H	VAL92

site_id	AE5
Number of Residues	5
Details	binding site for residue MG H 402

Chain	Residue
H	ARG203
H	ASN213
H	ASP248
H	GLU260
H	ANP401

site_id	AE6
Number of Residues	5
Details	binding site for residue SO4 H 403

Chain	Residue
G	VAL92
H	ARG96
H	ARG102
H	ARG109
H	HOH534

site_id	AE7
Number of Residues	20
Details	binding site for Di-peptide ANP B 401 and ASN B 213

Chain	Residue
B	LYS100
B	VAL139
B	LYS141
B	VAL151
B	GLN177
B	GLU178
B	TYR179
B	ILE180
B	ASP187
B	ARG203
B	PHE210
B	ARG211
B	SER212
B	LEU214
B	HIS215
B	ARG216
B	LEU250
B	MET259
B	GLU260
B	MG402

site_id	AE8
Number of Residues	11
Details	binding site for Di-peptide SO4 B 403 and ARG B 102

Chain	Residue
A	ARG78
B	ARG96
B	ASP99
B	LYS100
B	LEU101
B	SER103
B	MET104
B	GLN105
B	LEU106
B	HOH509
B	HOH531

site_id	AE9
Number of Residues	10
Details	binding site for Di-peptide SO4 E 401 and ARG E 203

Chain	Residue
E	GLY185
E	CYS186
E	ASP187
E	ARG189
E	GLU202
E	ARG204
E	SER212
E	ASN213
E	LEU214
E	ALA219

site_id	AF1
Number of Residues	26
Details	binding site for Di-peptide ANP E 402 and GLY E 148

Chain	Residue
E	LYS141
E	GLY145
E	THR146
E	GLN147
E	ILE149
E	GLY150
E	VAL151
E	GLN177
E	GLU178
E	TYR179
E	ILE180
E	ASP187
E	PHE210
E	ARG211
E	SER212
E	ASN213
E	LEU250
E	MET259
E	MG403
E	HOH502
E	HOH508
E	HOH550
E	HOH559
E	HOH564
E	HOH573
E	HOH585

site_id	AF2
Number of Residues	12
Details	binding site for Di-peptide SO4 G 403 and ARG G 203

Chain	Residue
G	GLY185
G	CYS186
G	ASP187
G	ARG189
G	GLU202
G	ARG204
G	SER212
G	ASN213
G	LEU214
G	ALA219
G	HOH532
G	HOH576

site_id	AF3
Number of Residues	23
Details	binding site for Di-peptide ANP H 401 and ASN H 213

Chain	Residue
H	LYS100
H	VAL139
H	LYS141
H	VAL151
H	GLN177
H	GLU178
H	TYR179
H	ILE180
H	ASP187
H	ARG203
H	PHE210
H	ARG211
H	SER212
H	LEU214
H	HIS215
H	ARG216
H	GLY217
H	GLY218
H	LEU250
H	MET259
H	GLU260
H	MG402
H	HOH547

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	32
Details	BINDING: BINDING => ECO:0000305\|PubMed:23609986

Chain	Residue	Details
A	LYS141
C	GLU178
C	ASP187
C	ARG211
D	LYS141
D	GLU178
D	ASP187
D	ARG211
E	LYS141
E	GLU178
E	ASP187
A	GLU178
E	ARG211
F	LYS141
F	GLU178
F	ASP187
F	ARG211
G	LYS141
G	GLU178
G	ASP187
G	ARG211
H	LYS141
A	ASP187
H	GLU178
H	ASP187
H	ARG211
A	ARG211
B	LYS141
B	GLU178
B	ASP187
B	ARG211
C	LYS141

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_01552

Chain	Residue	Details
A	ASP248
D	ASP248
D	GLU260
D	ASN262
E	ASP248
E	GLU260
E	ASN262
F	ASP248
F	GLU260
F	ASN262
G	ASP248
A	GLU260
G	GLU260
G	ASN262
H	ASP248
H	GLU260
H	ASN262
A	ASN262
B	ASP248
B	GLU260
B	ASN262
C	ASP248
C	GLU260
C	ASN262

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