Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6KKM

Crystal structure of RbcL-Raf1 complex from Anabaena sp. PCC 7120

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004497molecular_functionmonooxygenase activity
A0009853biological_processphotorespiration
A0015977biological_processcarbon fixation
A0015979biological_processphotosynthesis
A0016491molecular_functionoxidoreductase activity
A0016829molecular_functionlyase activity
A0016984molecular_functionribulose-bisphosphate carboxylase activity
A0019253biological_processreductive pentose-phosphate cycle
A0031470cellular_componentcarboxysome
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0004497molecular_functionmonooxygenase activity
B0009853biological_processphotorespiration
B0015977biological_processcarbon fixation
B0015979biological_processphotosynthesis
B0016491molecular_functionoxidoreductase activity
B0016829molecular_functionlyase activity
B0016984molecular_functionribulose-bisphosphate carboxylase activity
B0019253biological_processreductive pentose-phosphate cycle
B0031470cellular_componentcarboxysome
B0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0004497molecular_functionmonooxygenase activity
C0009853biological_processphotorespiration
C0015977biological_processcarbon fixation
C0015979biological_processphotosynthesis
C0016491molecular_functionoxidoreductase activity
C0016829molecular_functionlyase activity
C0016984molecular_functionribulose-bisphosphate carboxylase activity
C0019253biological_processreductive pentose-phosphate cycle
C0031470cellular_componentcarboxysome
C0046872molecular_functionmetal ion binding
D0000287molecular_functionmagnesium ion binding
D0004497molecular_functionmonooxygenase activity
D0009853biological_processphotorespiration
D0015977biological_processcarbon fixation
D0015979biological_processphotosynthesis
D0016491molecular_functionoxidoreductase activity
D0016829molecular_functionlyase activity
D0016984molecular_functionribulose-bisphosphate carboxylase activity
D0019253biological_processreductive pentose-phosphate cycle
D0031470cellular_componentcarboxysome
D0046872molecular_functionmetal ion binding
E0005737cellular_componentcytoplasm
E0015977biological_processcarbon fixation
E0015979biological_processphotosynthesis
E0110102biological_processribulose bisphosphate carboxylase complex assembly
F0005737cellular_componentcytoplasm
F0015977biological_processcarbon fixation
F0015979biological_processphotosynthesis
F0110102biological_processribulose bisphosphate carboxylase complex assembly
G0005737cellular_componentcytoplasm
G0015977biological_processcarbon fixation
G0015979biological_processphotosynthesis
G0110102biological_processribulose bisphosphate carboxylase complex assembly
H0005737cellular_componentcytoplasm
H0015977biological_processcarbon fixation
H0015979biological_processphotosynthesis
H0110102biological_processribulose bisphosphate carboxylase complex assembly
Functional Information from PROSITE/UniProt
site_idPS00157
Number of Residues9
DetailsRUBISCO_LARGE Ribulose bisphosphate carboxylase large chain active site. GlDFtKdDE
ChainResidueDetails
AGLY197-GLU205

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues126
DetailsRegion: {"description":"C-terminal beta-sheet","evidences":[{"source":"HAMAP-Rule","id":"MF_00856","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"32451445","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01338","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"description":"in homodimeric partner","evidences":[{"source":"HAMAP-Rule","id":"MF_01338","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01338","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"description":"via carbamate group","evidences":[{"source":"HAMAP-Rule","id":"MF_01338","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_01338","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"N6-carboxylysine","evidences":[{"source":"HAMAP-Rule","id":"MF_01338","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

PDB statisticsPDBj update infoContact PDBjnumon