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

2FGK

Crystal structure of the ABC-cassette E631Q mutant of HlyB with bound ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016887molecular_functionATP hydrolysis activity
B0005524molecular_functionATP binding
B0016887molecular_functionATP hydrolysis activity
C0005524molecular_functionATP binding
C0016887molecular_functionATP hydrolysis activity
D0005524molecular_functionATP binding
D0016887molecular_functionATP hydrolysis activity
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ATP A 800
ChainResidue
AHOH10
ASER509
ATHR510
AHIS662
BGLY605
BSER607
BGLY608
BGLY609
BGLN610
AHOH36
ATYR477
AILE484
ASER504
AGLY505
ASER506
AGLY507
ALYS508

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ATP B 801
ChainResidue
AGLY605
ASER607
AGLY609
AGLN610
BHOH120
BTYR477
BILE484
BSER504
BGLY505
BSER506
BGLY507
BLYS508
BSER509
BTHR510
BGLN631
BHIS662

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ATP C 802
ChainResidue
CHOH8
CHOH19
CTYR477
CILE484
CSER504
CGLY505
CSER506
CGLY507
CLYS508
CSER509
CTHR510
CGLN550
CHIS662
DGLY605
DSER607
DGLY609
DGLN610

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ATP D 803
ChainResidue
CGLY605
CSER607
CGLY608
CGLY609
CGLN610
DHOH65
DTYR477
DSER504
DGLY505
DSER506
DGLY507
DLYS508
DSER509
DTHR510
DLYS513
DHIS662

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGQRQRIAIARAL
ChainResidueDetails
ALEU606-LEU620

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00362, ECO:0000255|PROSITE-ProRule:PRU00434
ChainResidueDetails
AGLY502
BGLY502
CGLY502
DGLY502

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon