Skip to main content
. 2006 Mar 14;103(12):4433–4438. doi: 10.1073/pnas.0600433103

Table 3.

Known GroEL substrate proteins

Protein Swiss-Prot ID PDB* Organism NB NM NO§
Rubisco RBL2_RHORU 5RUB Rhodospirillum rubrum 11 0 0
Bacterial luciferase α-chain LUXA_VIBHA 1LUC Vibrio harveyi 8 0 0
Bacterial luciferase β-chain LUXB_VIBHA 1LUC Vibrio harveyi 4 0 0
mMDH MDHM_PIG 1MLD Sus scrofa 6 0 0
cMDH MDHC_PIG 5MDH Sus scrofa 6 1 0
Subtilisin BPN′ precursor SUBT_BACAM 1GNS Bacillus amyloliquefaciens 4 0 0
Barnase RNBR_BACAM 1A2P Bacillus amyloliquefaciens 2 0 0
Dihydrofolate reductase DYR_CHICK 8DFR Gallus gallus 4 0 0
Lysozyme C precursor LYSC_CHICK 1H87 Gallus gallus 3 0 0
Rhodanese THTR_BOVIN 1BOI Bos taurus 6 0 0
α-Lactalbumin precursor LALBA_HUMAN 1B9O Homo sapiens 5 1 1
α-Lactalbumin precursor LALBA_BOVIN 1F6R Bos taurus 5 0 0

*Protein Data Bank ID code of substrate proteins.

Number of GroES-type SPBM for which the GroEL-accessible area is determined.

Number of GroEL-accessible SPBM in monomeric native structures.

§Number of GroEL-accessible SPBM in oligomeric native structures.

A single chain is resolved in the crystal structure of the human α-lactalbumin, a heterodimer.

Six chains are present in the crystallographic asymmetric unit of the bovine α-lactalbumin, a heterodimer.