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1E3V

Crystal structure of ketosteroid isomerase from Psedomonas putida complexed with deoxycholate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004769molecular_functionsteroid delta-isomerase activity
A0008202biological_processsteroid metabolic process
A0016853molecular_functionisomerase activity
B0004769molecular_functionsteroid delta-isomerase activity
B0008202biological_processsteroid metabolic process
B0016853molecular_functionisomerase activity
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE DXC A 801
ChainResidue
ATYR16
BTRP92
BGLN95
BVAL127
AASP40
APHE56
AGLY60
AASP103
AMET116
AALA118
AHOH2024
AHOH2033

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE DXC B 801
ChainResidue
ATRP92
AGLN95
AVAL127
BTYR16
BASP40
BPHE56
BGLY60
BASP103
BMET116
BALA118
BHOH2044
BHOH2045

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor
ChainResidueDetails
ATYR16
BTYR16

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASP40
BASP40

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:11007792
ChainResidueDetails
AASP103
BASP103

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 11007792
ChainResidueDetails
AASP40
AASP100
ATYR16

site_idMCSA1
Number of Residues4
DetailsM-CSA 349
ChainResidueDetails
ATYR16proton acceptor, proton donor
AASP40proton acceptor, proton donor
AASP100electrostatic stabiliser
AASP103electrostatic stabiliser

site_idMCSA2
Number of Residues4
DetailsM-CSA 349
ChainResidueDetails
BTYR16proton acceptor, proton donor
BASP40proton acceptor, proton donor
BASP100electrostatic stabiliser
BASP103electrostatic stabiliser

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PDB entries from 2024-10-02

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