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3TY3

Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe bound to glycyl-glycyl-glycine

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0008652biological_processamino acid biosynthetic process
A0009085biological_processlysine biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0019878biological_processlysine biosynthetic process via aminoadipic acid
A0046872molecular_functionmetal ion binding
A0047046molecular_functionhomoisocitrate dehydrogenase activity
A0051287molecular_functionNAD binding
B0000287molecular_functionmagnesium ion binding
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0008652biological_processamino acid biosynthetic process
B0009085biological_processlysine biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0019878biological_processlysine biosynthetic process via aminoadipic acid
B0046872molecular_functionmetal ion binding
B0047046molecular_functionhomoisocitrate dehydrogenase activity
B0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GGG A 363
ChainResidue
AGLY77
AHOH454
AHOH477
AHOH487
AHOH537
AALA78
AVAL79
ASER81
AILE93
AARG97
AGLU285
APRO286
AHIS288

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 364
ChainResidue
AILE17
AALA300
AASN301
AASP342

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 3968
ChainResidue
AASP44
ALEU45
AASP46
AARG62
ATHR63
AARG66
AHOH502
AHOH535
BARG27
BASN350

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 3969
ChainResidue
AHIS186
ALYS188
ACYS244
AHOH412
AHOH591

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GGG B 363
ChainResidue
BGLY77
BALA78
BVAL79
BSER81
BILE93
BARG97
BGLU285
BPRO286
BVAL287
BHIS288

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 364
ChainResidue
BLYS110
BASP121
BARG174
BILE177
BARG178
BSER184

Functional Information from PROSITE/UniProt
site_idPS00470
Number of Residues20
DetailsIDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLYGDIlSDgaAsli.GSLGL
ChainResidueDetails
AASN252-LEU271

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q72IW9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"Q72IW9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18257517","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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