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1CQS

CRYSTAL STRUCTURE OF D103E MUTANT WITH EQUILENINEOF KSI IN PSEUDOMONAS PUTIDA

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 Residues6
DetailsBINDING SITE FOR RESIDUE EQU A 801
ChainResidue
ATYR16
AASN40
AGLU103
ATRP120
BTRP292
BASN293

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EQU B 802
ChainResidue
BMET290
BGLU303
AASN93
BTYR216
BASN240

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor
ChainResidueDetails
ATYR16
BTYR216

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASN40
BASN240

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:11007792
ChainResidueDetails
AGLU103
BGLU303

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1e3v
ChainResidueDetails
AGLU103
AASN40
ATYR32
ATYR16
ATYR57

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1e3v
ChainResidueDetails
BTYR216
BTYR257
BASN240
BGLU303
BTYR232

site_idMCSA1
Number of Residues4
DetailsM-CSA 349
ChainResidueDetails
ATYR16proton acceptor, proton donor
AASN40proton acceptor, proton donor
AASP100electrostatic stabiliser
AGLU103electrostatic stabiliser

site_idMCSA2
Number of Residues4
DetailsM-CSA 349
ChainResidueDetails
BTYR216proton acceptor, proton donor
BASN240proton acceptor, proton donor
BASP300electrostatic stabiliser
BGLU303electrostatic stabiliser

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PDB entries from 2024-05-01

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