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2IXG

Crystal structure of the ATPase domain of TAP1 with ATP (S621A, G622V, D645N mutant)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016887molecular_functionATP hydrolysis activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ATP A 1
ChainResidue
ATYR489
ATHR523
AGLN678
AVAL497
APRO516
AASN517
AGLY518
ASER519
AGLY520
ALYS521
ASER522

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 2
ChainResidue
AHIS555
AALA560
AARG632
AARG636
AARG660
AHOH2021

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LAVGQRQAVALARAL
ChainResidueDetails
ALEU620-LEU634

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434, ECO:0000269|PubMed:17018292, ECO:0007744|PDB:2IXE, ECO:0007744|PDB:2IXF, ECO:0007744|PDB:2IXG, ECO:0007744|PDB:4K8O
ChainResidueDetails
AGLY515

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17018292, ECO:0000269|PubMed:25377891, ECO:0007744|PDB:2IXE, ECO:0007744|PDB:2IXF, ECO:0007744|PDB:4K8O
ChainResidueDetails
ASER522
AASN618

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:17018292, ECO:0000269|PubMed:25377891, ECO:0007744|PDB:2IXE, ECO:0007744|PDB:2IXG, ECO:0007744|PDB:4K8O
ChainResidueDetails
AGLN678

224572

PDB entries from 2024-09-04

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