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2FGJ

Crystal structure of the ABC-cassette H662A 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 Residues19
DetailsBINDING SITE FOR RESIDUE ATP A 800
ChainResidue
AHOH29
ALYS508
ASER509
ATHR510
ALYS513
BGLY605
BLEU606
BSER607
BGLY608
BGLY609
BGLN610
AHOH31
AHOH115
ATYR477
AILE484
ASER504
AGLY505
ASER506
AGLY507

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ATP B 801
ChainResidue
AGLY605
ASER607
AGLY608
AGLY609
AGLN610
BHOH1
BHOH107
BHOH172
BTYR477
BILE484
BSER504
BGLY505
BSER506
BGLY507
BLYS508
BSER509
BTHR510

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ATP C 802
ChainResidue
CHOH95
CHOH104
CHOH143
CHOH181
CTYR477
CILE484
CSER504
CGLY505
CSER506
CGLY507
CLYS508
CSER509
CTHR510
DGLY605
DSER607
DGLY609
DGLN610

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ATP D 803
ChainResidue
CGLY605
CSER607
CGLY609
CGLN610
DHOH97
DHOH142
DHOH179
DTYR477
DILE484
DARG503
DSER504
DGLY505
DSER506
DGLY507
DLYS508
DSER509
DTHR510

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

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