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4MU1

The structure of wt A. thaliana IGPD2 in complex with Mn2+, imidazole, and sulfate at 1.5 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000105biological_processhistidine biosynthetic process
A0004424molecular_functionimidazoleglycerol-phosphate dehydratase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 301
ChainResidue
AHIS47
AHIS74
AHIS169
AGLU173
AIMD303
AHOH404

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 302
ChainResidue
AHIS170
AIMD303
AHOH401
AHIS73
AGLU77
AHIS145

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE IMD A 303
ChainResidue
AHIS73
AGLU77
ALEU107
AHIS170
AGLU173
AMN301
AMN302
AHOH401

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 304
ChainResidue
AARG161
AARG161
AARG161

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 305
ChainResidue
AGLN51
AHIS55
AARG99
ALYS177
AHOH495

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 306
ChainResidue
AGLU18
AASN23
AASN23
ASER25
AARG63
AHOH528
AHOH542

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 307
ChainResidue
ALEU88
AARG94
ALEU118
ASER119
AGLY120
ASER154
AGLY155
AHOH503

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 308
ChainResidue
AGLU93
AARG94
ALYS95
AHOH444
AHOH565

Functional Information from PROSITE/UniProt
site_idPS00954
Number of Residues14
DetailsIGP_DEHYDRATASE_1 Imidazoleglycerol-phosphate dehydratase signature 1. IDdHHtnEdvALAI
ChainResidueDetails
AILE70-ILE83

site_idPS00955
Number of Residues13
DetailsIGP_DEHYDRATASE_2 Imidazoleglycerol-phosphate dehydratase signature 2. GkNsHHiiEAtFK
ChainResidueDetails
AGLY165-LYS177

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:27717128, ECO:0007744|PDB:5EKW, ECO:0007744|PDB:5EL9, ECO:0007744|PDB:5ELW
ChainResidueDetails
AGLU21

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: 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
ChainResidueDetails
AGLU173
AHIS47
AHIS74
AHIS169

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: 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
ChainResidueDetails
AGLU77
AHIS145
AHIS170
AHIS73

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: 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
ChainResidueDetails
AARG99

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: 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
ChainResidueDetails
ASER199
AARG121

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PDB entries from 2024-06-12

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