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4GQU

Crystal structure of HisB from Mycobacterium tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0000105biological_processhistidine biosynthetic process
A0004424molecular_functionimidazoleglycerol-phosphate dehydratase activity
A0005737cellular_componentcytoplasm
A0008652biological_processamino acid biosynthetic process
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 301
ChainResidue
AHIS73
AGLU77
AHIS152
AHIS177
AHOH425
AHOH505

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 302
ChainResidue
AGLU180
AHOH438
AHOH506
AHIS47
AHIS74
AHIS176

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN A 303
ChainResidue
AARG168
AARG168
AARG168

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MN A 304
ChainResidue
AARG151
AEDO305

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 305
ChainResidue
AGLY128
AARG151
AMN304

Functional Information from PROSITE/UniProt
site_idPS00954
Number of Residues14
DetailsIGP_DEHYDRATASE_1 Imidazoleglycerol-phosphate dehydratase signature 1. IEaHHtiEdtAIAL
ChainResidueDetails
AILE70-LEU83

site_idPS00955
Number of Residues13
DetailsIGP_DEHYDRATASE_2 Imidazoleglycerol-phosphate dehydratase signature 2. GrDpHHitEAqYK
ChainResidueDetails
AGLY172-LYS184

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O23346
ChainResidueDetails
ASER205
AGLU21
AARG99
AARG121

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:24311587, ECO:0007744|PDB:4GQU
ChainResidueDetails
AGLU77
AHIS152
AHIS176
AHIS177
AGLU180
AHIS47
AHIS73
AHIS74

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PDB entries from 2024-04-17

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