Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4F0M

UNACTIVATED RUBISCO with MAGNESIUM AND A WATER MOLECULE BOUND

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004497molecular_functionmonooxygenase activity
A0009507cellular_componentchloroplast
A0015977biological_processcarbon fixation
A0015979biological_processphotosynthesis
A0016829molecular_functionlyase activity
A0016984molecular_functionribulose-bisphosphate carboxylase activity
A0019253biological_processreductive pentose-phosphate cycle
A0046872molecular_functionmetal ion binding
B0009507cellular_componentchloroplast
B0015977biological_processcarbon fixation
B0015979biological_processphotosynthesis
B0016984molecular_functionribulose-bisphosphate carboxylase activity
B0019253biological_processreductive pentose-phosphate cycle
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 501
ChainResidue
AHIS302
AHOH702
AHOH735
AHOH751

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 502
ChainResidue
AHIS315
AHIS315
AGLN312
AGLN312
ALYS313
AASN314
AASN314

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 701
ChainResidue
BGLN614
BGLN614
BGLN614
BGLN614

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 702
ChainResidue
AARG170
APHE229
AHOH810
BARG544
BHOH809
BHOH816
BHOH821

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 703
ChainResidue
AALA239
AALA240
AHOH761
BPRO607
BPHE609
BTYR628
BGLU634

Functional Information from PROSITE/UniProt
site_idPS00157
Number of Residues9
DetailsRUBISCO_LARGE Ribulose bisphosphate carboxylase large chain active site. GlDFvKdDE
ChainResidueDetails
AGLY205-GLU213

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01338
ChainResidueDetails
ALYS184
AHIS302

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: in homodimeric partner => ECO:0000255|HAMAP-Rule:MF_01338
ChainResidueDetails
AASN132

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01338
ChainResidueDetails
ATHR182
ALYS186
AASP212
AGLU213
AARG303
AHIS335
ASER387

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: via carbamate group => ECO:0000255|HAMAP-Rule:MF_01338
ChainResidueDetails
ALYS210

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01338
ChainResidueDetails
ALYS342

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:23112176, ECO:0007744|PDB:4F0H, ECO:0007744|PDB:4F0K, ECO:0007744|PDB:4F0M
ChainResidueDetails
ASNC181
ASNC460

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-carboxylysine => ECO:0000255|HAMAP-Rule:MF_01338
ChainResidueDetails
ALYS210

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon