5EL9

A. thaliana IGPD2 in complex with the triazole-phosphonate inhibitor, (S)-C348, to 1.1A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000105	biological_process	L-histidine biosynthetic process
A	0004424	molecular_function	imidazoleglycerol-phosphate dehydratase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue MN A 301

Chain	Residue
A	HIS73
A	GLU77
A	HIS145
A	HIS170
A	5DL303
A	HOH536

---

site_id	AC2
Number of Residues	5
Details	binding site for residue MN A 302

Chain	Residue
A	GLU173
A	5DL303
A	HIS47
A	HIS74
A	HIS169

---

site_id	AC3
Number of Residues	17
Details	binding site for residue 5DL A 303

Chain	Residue
A	GLU21
A	HIS47
A	HIS73
A	HIS74
A	GLU77
A	ARG99
A	ARG121
A	HIS169
A	HIS170
A	GLU173
A	LYS177
A	SER199
A	LYS201
A	MN301
A	MN302
A	HOH459
A	HOH536

---

site_id	AC4
Number of Residues	12
Details	binding site for residue TRS A 304

Chain	Residue
A	ASP102
A	ASP102
A	ASP102
A	PHE103
A	PHE103
A	PHE103
A	GLN185
A	GLN185
A	GLN185
A	HOH503
A	HOH503
A	HOH503

---

site_id	AC5
Number of Residues	8
Details	binding site for residue EDO A 305

Chain	Residue
A	GLU18
A	ASN23
A	ASN23
A	SER25
A	ARG63
A	HOH458
A	HOH458
A	HOH505

---

site_id	AC6
Number of Residues	6
Details	binding site for residue EDO A 306

Chain	Residue
A	SER36
A	ASP37
A	SER38
A	ASP50
A	HOH405
A	HOH532

---

site_id	AC7
Number of Residues	10
Details	binding site for residue EDO A 307

Chain	Residue
A	PRO122
A	PRO122
A	TYR123
A	GLN148
A	ASN152
A	ASN152
A	HOH465
A	HOH465
A	HOH481
A	HOH481

---

site_id	AC8
Number of Residues	4
Details	binding site for residue EDO A 308

Chain	Residue
A	ARG11
A	ASP31
A	LYS95
A	HOH420

---

site_id	AC9
Number of Residues	4
Details	binding site for residue EDO A 309

Chain	Residue
A	ASN127
A	GLU129
A	GLN162
A	HOH486

---

site_id	AD1
Number of Residues	7
Details	binding site for residue EDO A 310

Chain	Residue
A	LEU128
A	GLU129
A	ILE130
A	THR140
A	GLN141
A	HOH409
A	HOH598

---

site_id	AD2
Number of Residues	7
Details	binding site for residue EDO A 311

Chain	Residue
A	ASN98
A	PHE100
A	PHE103
A	ARG181
A	GLN185
A	HOH476
A	HOH527

---

Functional Information from PROSITE/UniProt

site_id	PS00954
Number of Residues	14
Details	IGP_DEHYDRATASE_1 Imidazoleglycerol-phosphate dehydratase signature 1. IDdHHtnEdvALAI

Chain	Residue	Details
A	ILE70-ILE83

---

site_id	PS00955
Number of Residues	13
Details	IGP_DEHYDRATASE_2 Imidazoleglycerol-phosphate dehydratase signature 2. GkNsHHiiEAtFK

Chain	Residue	Details
A	GLY165-LYS177

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:27717128, ECO:0007744|PDB:5EKW, ECO:0007744|PDB:5EL9, ECO:0007744|PDB:5ELW

Chain	Residue	Details
A	GLU21

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:26095028, ECO:0000269|PubMed:27717128, ECO:0007744|PDB:4MU0, ECO:0007744|PDB:4MU1, ECO:0007744|PDB:4MU4, ECO:0007744|PDB:4QNJ, ECO:0007744|PDB:4QNK, ECO:0007744|PDB:5EKW, ECO:0007744|PDB:5EL9, ECO:0007744|PDB:5ELW

Chain	Residue	Details
A	HIS47
A	HIS74
A	HIS169
A	GLU173

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:26095028, ECO:0000269|PubMed:27717128, ECO:0007744|PDB:4MU0, ECO:0007744|PDB:4MU3, ECO:0007744|PDB:4MU4, ECO:0007744|PDB:4QNJ, ECO:0007744|PDB:4QNK, ECO:0007744|PDB:5ELW

Chain	Residue	Details
A	HIS73
A	GLU77
A	HIS145
A	HIS170

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:26095028, ECO:0000269|PubMed:27717128, ECO:0007744|PDB:4MU3, ECO:0007744|PDB:4MU4, ECO:0007744|PDB:4QNK, ECO:0007744|PDB:5EKW, ECO:0007744|PDB:5EL9, ECO:0007744|PDB:5ELW

Chain	Residue	Details
A	ARG99

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:26095028, ECO:0000269|PubMed:27717128, ECO:0007744|PDB:4MU4, ECO:0007744|PDB:5EKW, ECO:0007744|PDB:5EL9, ECO:0007744|PDB:5ELW

Chain	Residue	Details
A	ARG121
A	SER199

---