2ZXI

Structure of Aquifex aeolicus GidA in the form II crystal

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002098	biological_process	tRNA wobble uridine modification
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0008033	biological_process	tRNA processing
A	0030488	biological_process	tRNA methylation
A	0050660	molecular_function	flavin adenine dinucleotide binding
B	0002098	biological_process	tRNA wobble uridine modification
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0008033	biological_process	tRNA processing
B	0030488	biological_process	tRNA methylation
B	0050660	molecular_function	flavin adenine dinucleotide binding
C	0002098	biological_process	tRNA wobble uridine modification
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0008033	biological_process	tRNA processing
C	0030488	biological_process	tRNA methylation
C	0050660	molecular_function	flavin adenine dinucleotide binding
D	0002098	biological_process	tRNA wobble uridine modification
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0008033	biological_process	tRNA processing
D	0030488	biological_process	tRNA methylation
D	0050660	molecular_function	flavin adenine dinucleotide binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	39
Details	BINDING SITE FOR RESIDUE FAD A 618

Chain	Residue
A	ILE13
A	CYS48
A	LYS57
A	GLU124
A	GLU125
A	VAL126
A	THR155
A	THR156
A	GLY157
A	THR158
A	PHE159
A	GLY14
A	SER181
A	THR200
A	GLY201
A	TYR348
A	ILE350
A	GLY376
A	ASN377
A	THR382
A	GLY383
A	ALA387
A	GLY15
A	ARG434
A	HOH619
A	HOH623
A	HOH626
A	HOH635
A	HOH655
A	HOH659
A	HOH665
A	HOH672
A	HOH713
A	GLY16
A	HIS17
A	ALA18
A	PHE36
A	VAL37
A	LEU38

---

site_id	AC2
Number of Residues	42
Details	BINDING SITE FOR RESIDUE FAD B 618

Chain	Residue
B	ILE13
B	GLY14
B	GLY15
B	GLY16
B	HIS17
B	ALA18
B	VAL37
B	LEU38
B	CYS48
B	LYS57
B	GLU124
B	GLU125
B	VAL126
B	THR155
B	THR156
B	GLY157
B	THR158
B	PHE159
B	ARG175
B	SER181
B	THR200
B	GLY201
B	TYR348
B	ILE350
B	GLY376
B	ASN377
B	THR382
B	GLY383
B	TYR384
B	ALA387
B	ARG434
B	HOH620
B	HOH621
B	HOH628
B	HOH637
B	HOH640
B	HOH647
B	HOH649
B	HOH675
B	HOH698
B	HOH850
B	HOH907

---

site_id	AC3
Number of Residues	40
Details	BINDING SITE FOR RESIDUE FAD C 618

Chain	Residue
C	ARG175
C	SER181
C	THR200
C	GLY201
C	TYR348
C	ILE350
C	GLY376
C	ASN377
C	THR382
C	GLY383
C	TYR384
C	ALA387
C	ARG434
C	HOH619
C	HOH620
C	HOH622
C	HOH626
C	HOH628
C	HOH644
C	HOH649
C	HOH653
C	HOH654
C	ILE13
C	GLY14
C	GLY15
C	GLY16
C	HIS17
C	ALA18
C	VAL37
C	LEU38
C	CYS48
C	LYS57
C	GLU124
C	GLU125
C	VAL126
C	THR155
C	THR156
C	GLY157
C	THR158
C	PHE159

---

site_id	AC4
Number of Residues	40
Details	BINDING SITE FOR RESIDUE FAD D 618

Chain	Residue
D	ILE13
D	GLY14
D	GLY15
D	GLY16
D	HIS17
D	ALA18
D	PHE36
D	VAL37
D	LEU38
D	CYS48
D	LYS57
D	GLU124
D	GLU125
D	VAL126
D	THR155
D	THR156
D	GLY157
D	THR158
D	PHE159
D	SER181
D	THR200
D	GLY201
D	TYR348
D	ILE350
D	GLY376
D	ASN377
D	THR382
D	GLY383
D	ALA387
D	ARG434
D	HOH620
D	HOH624
D	HOH625
D	HOH637
D	HOH649
D	HOH651
D	HOH680
D	HOH689
D	HOH708
D	HOH763

---

Functional Information from PROSITE/UniProt

site_id	PS01280
Number of Residues	15
Details	GIDA_1 Glucose inhibited division protein A family signature 1. GPrYCPSIEdKIvKF

Chain	Residue	Details
A	GLY280-PHE294

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site_id	PS01281
Number of Residues	24
Details	GIDA_2 Glucose inhibited division protein A family signature 2. AGNfNGttGYeEAAGQGIVAGINA

Chain	Residue	Details
A	ALA375-ALA398

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269|Ref.2

Chain	Residue	Details
A	GLY14
C	VAL126
C	SER181
C	ASN377
D	GLY14
D	VAL126
D	SER181
D	ASN377
A	VAL126
A	SER181
A	ASN377
B	GLY14
B	VAL126
B	SER181
B	ASN377
C	GLY14

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255

Chain	Residue	Details
A	GLY280
B	GLY280
C	GLY280
D	GLY280

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