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1Q0H

Crystal structure of selenomethionine-labelled DXR in complex with fosmidomycin

Functional Information from GO Data
ChainGOidnamespacecontents
A0008299biological_processisoprenoid biosynthetic process
A0019288biological_processisopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway
A0030145molecular_functionmanganese ion binding
A0030604molecular_function1-deoxy-D-xylulose-5-phosphate reductoisomerase activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0070402molecular_functionNADPH binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE FOM A 400
ChainResidue
ASER151
AMSE276
AHOH415
AHOH464
AHOH653
AGLU152
AGLY185
ASER186
AHIS209
ASER222
AASN227
ALYS228
AGLU231

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE NDP A 401
ChainResidue
AGLY8
ATHR10
AGLY11
ASER12
AILE13
AALA35
AGLY36
ALYS37
AASN38
AASP57
AILE101
AVAL102
AMSE214
AGLY215
AARG216
ALYS217
AHOH413
AHOH429
AHOH559
AHOH581
AHOH587
AHOH618
AHOH647

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CIT A 402
ChainResidue
ACYS15
AARG41
AARG352
AALA397
ASER398
AHOH483
AHOH629

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues17
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15567415","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Q0Q","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12621040","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ONO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ONP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

251174

PDB entries from 2026-03-25

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