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4G09

The crystal structure of the C366S mutant of HDH from Brucella suis in complex with a substituted benzyl ketone

Functional Information from GO Data
ChainGOidnamespacecontents
A0000105biological_processL-histidine biosynthetic process
A0004399molecular_functionhistidinol dehydrogenase activity
A0008270molecular_functionzinc ion binding
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0046872molecular_functionmetal ion binding
A0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
AHIS262
AASP361
AHIS420
ADMS504
A0VD505

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 502
ChainResidue
AASP313
AASP316
AHIS433
AHIS436

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 503
ChainResidue
APHE56
AGLY189
AGLN191
AASN214
AHOH613
AHOH797

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE DMS A 504
ChainResidue
AGLN259
AHIS262
AGLU357
AVAL358
AASP361
AHIS420
AZN501
A0VD505

site_idAC5
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 0VD A 505
ChainResidue
APRO132
AALA136
ATYR138
ASER140
AHIS262
AGLU327
AHIS328
AGLU357
AASP361
ATYR362
AHIS368
AGLU415
ALEU417
AHIS420
AZN501
ADMS504

Functional Information from PROSITE/UniProt
site_idPS00611
Number of Residues33
DetailsHISOL_DEHYDROGENASE Histidinol dehydrogenase signature. IDmi.AGPSEVLIVAdkdNnpdw..IAADLLAqaEH
ChainResidueDetails
AILE230-HIS262

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01024
ChainResidueDetails
AGLU327
AHIS328

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01024
ChainResidueDetails
ATYR130
AHIS420
AGLN191
AASN214
ASER237
AGLN259
AHIS262
AHIS328
AASP361
AGLU415

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PDB entries from 2024-07-24

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