Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5Y0T

Crystal structure of Thermotoga maritima TmcAL bound with alpha-thio ATP(Form II)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000049	molecular_function	tRNA binding
A	0000166	molecular_function	nucleotide binding
A	0003723	molecular_function	RNA binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006400	biological_process	tRNA modification
A	0008033	biological_process	tRNA processing
A	0016874	molecular_function	ligase activity
A	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
B	0000049	molecular_function	tRNA binding
B	0000166	molecular_function	nucleotide binding
B	0003723	molecular_function	RNA binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006400	biological_process	tRNA modification
B	0008033	biological_process	tRNA processing
B	0016874	molecular_function	ligase activity
B	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
C	0000049	molecular_function	tRNA binding
C	0000166	molecular_function	nucleotide binding
C	0003723	molecular_function	RNA binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006400	biological_process	tRNA modification
C	0008033	biological_process	tRNA processing
C	0016874	molecular_function	ligase activity
C	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
D	0000049	molecular_function	tRNA binding
D	0000166	molecular_function	nucleotide binding
D	0003723	molecular_function	RNA binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0006400	biological_process	tRNA modification
D	0008033	biological_process	tRNA processing
D	0016874	molecular_function	ligase activity
D	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	binding site for residue TAT A 1001

Chain	Residue
A	GLU9
A	ILE191
A	ARG193
A	VAL194
A	SER209
A	ALA210
A	HOH1106
A	HOH1114
A	HOH1116
A	HOH1123
A	HOH1134
A	TYR10
A	HOH1144
A	HOH1199
A	HOH1217
A	HIS14
A	GLY16
A	HIS17
A	HIS20
A	PHE101
A	GLY102
A	ASN168

site_id	AC2
Number of Residues	4
Details	binding site for residue EDO A 1002

Chain	Residue
A	GLY80
A	GLY81
A	LYS181
A	ASN330

site_id	AC3
Number of Residues	7
Details	binding site for residue EDO A 1003

Chain	Residue
A	LYS332
A	GLN335
A	LEU359
A	PRO378
A	VAL379
A	HOH1162
A	HOH1258

site_id	AC4
Number of Residues	7
Details	binding site for residue EDO A 1004

Chain	Residue
A	PHE256
A	PHE401
A	HOH1118
A	HOH1154
A	HOH1211
B	PHE401
B	HOH1165

site_id	AC5
Number of Residues	22
Details	binding site for residue TAT B 1001

Chain	Residue
B	GLU9
B	TYR10
B	HIS14
B	GLY16
B	HIS17
B	HIS20
B	PHE101
B	GLY102
B	ASN168
B	ILE191
B	ARG193
B	VAL194
B	SER209
B	ALA210
B	HOH1104
B	HOH1105
B	HOH1112
B	HOH1121
B	HOH1147
B	HOH1154
B	HOH1161
B	HOH1193

site_id	AC6
Number of Residues	6
Details	binding site for residue EDO B 1002

Chain	Residue
B	PHE319
B	GLU320
B	ASN322
B	PHE325
B	LYS393
B	HOH1107

site_id	AC7
Number of Residues	4
Details	binding site for residue EDO B 1003

Chain	Residue
B	LYS332
B	GLN335
B	LEU359
B	PRO378

site_id	AC8
Number of Residues	3
Details	binding site for residue EDO B 1004

Chain	Residue
B	ILE182
B	THR331
B	LYS332

site_id	AC9
Number of Residues	18
Details	binding site for residue TAT C 1001

Chain	Residue
C	GLU9
C	TYR10
C	HIS14
C	GLY16
C	HIS17
C	HIS20
C	PHE101
C	GLY102
C	ASN168
C	ARG193
C	VAL194
C	SER209
C	ALA210
C	HOH1107
C	HOH1136
C	HOH1138
C	HOH1227
C	HOH1271

site_id	AD1
Number of Residues	8
Details	binding site for residue EDO C 1002

Chain	Residue
C	HOH1127
C	HOH1152
C	PHE319
C	GLU320
C	VAL321
C	ASN322
C	PHE325
C	LYS393

site_id	AD2
Number of Residues	4
Details	binding site for residue EDO C 1003

Chain	Residue
C	GLY80
C	PHE84
C	LYS181
C	ASN330

site_id	AD3
Number of Residues	20
Details	binding site for residue TAT D 1001

Chain	Residue
D	GLU9
D	TYR10
D	HIS14
D	GLY16
D	HIS17
D	HIS20
D	ARG44
D	PHE101
D	GLY102
D	ARG193
D	VAL194
D	SER209
D	ALA210
D	1PE1003
D	HOH1121
D	HOH1123
D	HOH1130
D	HOH1133
D	HOH1159
D	HOH1175

site_id	AD4
Number of Residues	6
Details	binding site for residue EDO D 1002

Chain	Residue
D	PHE319
D	GLU320
D	ASN322
D	PHE325
D	LYS393
D	HOH1125

site_id	AD5
Number of Residues	10
Details	binding site for residue 1PE D 1003

Chain	Residue
D	GLU9
D	GLN43
D	ARG44
D	PHE82
D	SER167
D	ASN168
D	LEU171
D	ARG193
D	VAL194
D	TAT1001

site_id	AD6
Number of Residues	14
Details	binding site for Di-peptide PHE B 41 and CSD B 42

Chain	Residue
B	GLU9
B	ASN11
B	SER38
B	GLY39
B	ASN40
B	GLN43
B	ARG44
B	GLY45
B	GLU46
B	PHE319
B	ALA394
B	HOH1130
B	HOH1167
B	HOH1195

site_id	AD7
Number of Residues	14
Details	binding site for Di-peptide CSD B 42 and GLN B 43

Chain	Residue
B	GLU9
B	ASN11
B	PHE41
B	ARG44
B	GLY45
B	GLU46
B	ALA75
B	GLN77
B	ASP78
B	ALA79
B	PHE82
B	ARG312
B	HOH1130
B	HOH1195

site_id	AD8
Number of Residues	16
Details	binding site for Di-peptide ARG B 408 and CME B 409

Chain	Residue
A	ASP255
A	ARG262
A	GLN289
A	THR290
A	GLY291
A	HOH1166
B	SER399
B	MET400
B	PHE402
B	SER404
B	VAL405
B	GLU406
B	GLN407
B	GLY410
B	HOH1129
B	HOH1189

site_id	AD9
Number of Residues	11
Details	binding site for Di-peptide CME B 409 and GLY B 410

Chain	Residue
A	ARG288
A	GLN289
A	THR290
A	GLY291
B	VAL405
B	GLU406
B	GLN407
B	ARG408
B	GLU411
B	HOH1129
B	HOH1196

site_id	AE1
Number of Residues	13
Details	binding site for Di-peptide PHE C 41 and CSD C 42

Chain	Residue
C	GLU9
C	ASN11
C	SER38
C	GLY39
C	ASN40
C	GLN43
C	ARG44
C	GLY45
C	GLU46
C	ALA75
C	ALA394
C	HOH1169
C	HOH1225

site_id	AE2
Number of Residues	13
Details	binding site for Di-peptide CSD C 42 and GLN C 43

Chain	Residue
C	GLU9
C	ASN11
C	PHE41
C	ARG44
C	GLY45
C	GLU46
C	ALA75
C	GLN77
C	ASP78
C	ALA79
C	PHE82
C	ARG312
C	HOH1169

site_id	AE3
Number of Residues	14
Details	binding site for Di-peptide ARG C 408 and CME C 409

Chain	Residue
C	SER399
C	MET400
C	PHE402
C	VAL405
C	GLU406
C	GLN407
C	GLY410
C	HOH1140
C	HOH1174
D	ASP255
D	ARG262
D	GLN289
D	GLY291
D	HOH1134

site_id	AE4
Number of Residues	12
Details	binding site for Di-peptide CME C 409 and GLY C 410

Chain	Residue
C	VAL405
C	GLU406
C	GLN407
C	ARG408
C	GLU411
C	HOH1101
C	HOH1140
C	HOH1174
C	HOH1209
D	ARG288
D	GLN289
D	GLY291

site_id	AE5
Number of Residues	13
Details	binding site for Di-peptide PHE D 41 and CSD D 42

Chain	Residue
D	GLU9
D	ASN11
D	GLY39
D	ASN40
D	GLN43
D	ARG44
D	GLY45
D	GLU46
D	ALA75
D	LEU315
D	ALA394
D	HOH1113
D	HOH1194

site_id	AE6
Number of Residues	13
Details	binding site for Di-peptide CSD D 42 and GLN D 43

Chain	Residue
D	GLU9
D	ASN11
D	PHE41
D	ARG44
D	GLY45
D	GLU46
D	ALA75
D	GLN77
D	ASP78
D	ALA79
D	ARG312
D	1PE1003
D	HOH1113

site_id	AE7
Number of Residues	20
Details	binding site for Di-peptide ARG D 408 and CME D 409

Chain	Residue
A	HIS417
C	ASP255
C	ARG262
C	GLN289
C	THR290
C	GLY291
C	HOH1120
D	SER399
D	MET400
D	PHE402
D	PRO403
D	SER404
D	VAL405
D	GLU406
D	GLN407
D	GLY410
D	HOH1128
D	HOH1183
D	HOH1198
D	HOH1210

site_id	AE8
Number of Residues	15
Details	binding site for Di-peptide CME D 409 and GLY D 410

Chain	Residue
A	HIS417
C	ARG288
C	GLN289
C	THR290
C	GLY291
D	VAL405
D	GLU406
D	GLN407
D	ARG408
D	GLU411
D	HOH1109
D	HOH1128
D	HOH1196
D	HOH1198
D	HOH1210

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01539","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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