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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

2IV2

Reinterpretation of reduced form of formate dehydrogenase H from E. coli

Functional Information from GO Data
ChainGOidnamespacecontents
X0003954molecular_functionNADH dehydrogenase activity
X0005515molecular_functionprotein binding
X0005829cellular_componentcytosol
X0006007biological_processglucose catabolic process
X0008863molecular_functionformate dehydrogenase (NAD+) activity
X0009061biological_processanaerobic respiration
X0009326cellular_componentformate dehydrogenase complex
X0015942biological_processformate metabolic process
X0015944biological_processformate oxidation
X0016020cellular_componentmembrane
X0016491molecular_functionoxidoreductase activity
X0016903molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors
X0019628biological_processurate catabolic process
X0019645biological_processanaerobic electron transport chain
X0022904biological_processrespiratory electron transport chain
X0043546molecular_functionmolybdopterin cofactor binding
X0045333biological_processcellular respiration
X0046872molecular_functionmetal ion binding
X0051536molecular_functioniron-sulfur cluster binding
X0051539molecular_function4 iron, 4 sulfur cluster binding
X1990204cellular_componentoxidoreductase complex
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SF4 X 800
ChainResidue
XCYS8
XPRO182
XILE183
XTYR10
XCYS11
XSER13
XCYS15
XLEU41
XCYS42
XLYS44
XGLY45
site_idAC2
Number of Residues27
DetailsBINDING SITE FOR RESIDUE 2MD X 801
ChainResidue
XARG110
XGLY111
XTHR112
XCYS136
XGLN335
XGLY402
XGLU403
XASP404
XTHR408
XALA410
XGLN428
XASP429
XILE430
XTHR433
XSER445
XTHR446
XHIS451
XASP478
XCYS588
XSER590
XTYR678
XMGD802
XMO803
XUNX804
XHOH2155
XHOH2266
XHOH2267
site_idAC3
Number of Residues35
DetailsBINDING SITE FOR RESIDUE MGD X 802
ChainResidue
XLYS44
XPHE173
XGLY174
XTYR175
XASN176
XASP179
XSER180
XCYS201
XASP202
XPRO203
XARG204
XILE206
XGLY221
XASN223
XGLY296
XMET297
XPHE302
XGLY334
XTHR579
XVAL580
XARG581
XGLU582
XVAL583
XHIS585
XTYR586
XSER587
XTYR651
XLYS679
X2MD801
XMO803
XUNX804
XHOH2082
XHOH2084
XHOH2125
XHOH2259
site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MO X 803
ChainResidue
X2MD801
XMGD802
XUNX804
site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE UNX X 804
ChainResidue
XALA137
XGLY334
X2MD801
XMGD802
XMO803
Functional Information from PROSITE/UniProt
site_idPS00490
Number of Residues18
DetailsMOLYBDOPTERIN_PROK_2 Prokaryotic molybdopterin oxidoreductases signature 2. TkTAsaADVILPsTSwgE
ChainResidueDetails
XTHR433-GLU450
site_idPS00551
Number of Residues18
DetailsMOLYBDOPTERIN_PROK_1 Prokaryotic molybdopterin oxidoreductases signature 1. TvCpy.CASgCkInLvvd.N
ChainResidueDetails
XTHR6-ASN23
site_idPS00932
Number of Residues28
DetailsMOLYBDOPTERIN_PROK_3 Prokaryotic molybdopterin oxidoreductases signature 3. AkrlGIeDeAlVwVhSrkGkiitrAqVS
ChainResidueDetails
XALA615-SER642
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues55
DetailsDomain: {"description":"4Fe-4S Mo/W bis-MGD-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01004","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Electron donor/acceptor"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor"}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues23
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16830149","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9036855","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AA6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FDI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FDO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IV2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9036855","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AA6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FDI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FDO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16830149","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9036855","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AA6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FDI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IV2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16830149","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9036855","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FDI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FDO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IV2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsSite: {"description":"Important for catalytic activity"}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsNon-standard residue: {"description":"Selenocysteine","evidences":[{"source":"PubMed","id":"9036855","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1tmo
ChainResidueDetails
XASN132
site_idMCSA1
Number of Residues4
DetailsM-CSA 562
ChainResidueDetails

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PDB entries from 2025-10-22

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