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2PMK

Crystal structures of an isolated ABC-ATPase in complex with TNP-ADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016887molecular_functionATP hydrolysis activity
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE 128 A 301
ChainResidue
ATYR477
ALYS513
ATYR519
ATRP540
AARG543
AGLU689
ASER692
AGLU693
APRO694
AHOH713
AHOH721
APRO482
AHOH742
AHOH759
AHOH782
AHOH799
AHOH832
AHOH852
AILE484
AGLY505
ASER506
AGLY507
ALYS508
ASER509
ATHR510

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE ADP A 401
ChainResidue
ATYR477
AILE484
AARG503
ASER504
AGLY505
ASER506
AGLY507
ALYS508
ASER509
ATHR510
ALYS513
ATYR519
AGLU689
APRO694
AHOH713
AHOH721
AHOH742
AHOH759
AHOH782
AHOH801
AHOH832
AHOH852
AHOH898

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 Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00362, ECO:0000255|PROSITE-ProRule:PRU00434
ChainResidueDetails
AGLY502

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PDB entries from 2024-07-24

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