4MU3

The form A structure of an E21Q catalytic mutant of A. thaliana IGPD2 in complex with Mn2+ and a mixture of its substrate, 2R3S-IGP, and an inhibitor, 2S3S-IGP, to 1.12 A 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 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	GLN21

---

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

---